Genetic Variation at a Locus (TAM-1) for Submaxillary Gland Protease in the Mouse and Its Location on Chromosome 7

Electrophoretic and activity variants for a testosterone-induced esteroprotease have been discovered in submaxillary glands from inbred strains of mice. The enzyme is tentatively designated tamase (TAM-1) and the variant genetic locus is Tam-1. The alleles Tam-1^a and Tam-1^b determine electrophoretically distinct zones of tamase activity, while Tam-1^c produces no detectable enzyme activity. Data from recombinant inbred strains and B6AF₁ x B6 and B6D2F₁ x B6 backcrosses established linkage of Tam-1 to glucose phosphate isomerase (Gpi-1), pink-eyed dilution (p) and β-hemoglobin (Hbb) on chromosome 7. The gene order is Gpi-1—Tam-1—p—Hbb. Analysis of congenic resistant strains indicates that Tam-1 is closely linked to the minor histocompatibility locus, H-4. TAM-1 was not cross-reactive with antisera to mouse nerve growth factor, submaxillary renin, or tamases A and D.     

Glutamate oxalate transaminase (GOT) genetics in Mus musculus: Linkage,polymorphism, and phenotypes of the Got-2 and Got-1 loci

A comparison of electrophoretic patterns of F₁ and backcross progeny of two inbred strains of mice has revealed a new autosomal variant of the mitochondrial form of GOT. The loci controlling the production of the soluble and mitochondrial forms of GOT have been designated Got-1 and Got-2, respectively. The two alleles of the Got-2 locus have been designated Got-2 ^a and Got-2 ^b, which represent the slow- and fast-migrating electrophoretic forms. Twenty-seven inbred strains of mice have been classified for Got-2 ^a and Got-2 ^b. It has been demonstrated that the polymorphism of Got-2 is widely distributed in feral mice. Got-2 was shown to be linked to Es-1, and evidence is also presented for linkage between Got-2 and Es-2, Es-5, and oligosyndactyly (Os). The absence of linkage of Got-2 to seven other loci has also been demonstrated. GOT was expressed in vitro in cell lines derived from human and mouse tissues.     

Biochemical genetics of a new glucosephosphate isomerase allele (Gpi-1 c) from wild mice

We have found a new allele at the structural locus for glucosephosphate isomerase (called Gpi-1 ^c ) in a population of wild mice. The Gpi-1 ^c allele codes for an enzyme of greater cathodal electrophoretic mobility than either the Gpi-1 ^a or Gpi-1 ^b alleles found in the wild and in the SM/J and C57BL/6J inbred strains. Mice homozygous for Gpi-1 ^c have erythrocyte enzyme activity reduced to 33% of normal levels, altered pH profile, lowered heat stability, and normal K _m 's when compared with SM/J and C57BL/6J mice. The activity of the enzyme in brain, liver, and kidney is not so markedly lowered, although the electrophoretic mobility, pH profile, and heat stability are altered in these tissues. Deficiencies of erythrocyte glucosephosphate isomerase in man, to this level, can cause severe hemolytic anemia. Homozygotes for Gpi-1 ^c show only mild hematological symptoms. The frequency of Gpi-1 ^c in wild populations of mice is discussed and the occurrence of a further rare allele Gpi-1 ^d is reported.This work was supported by M.R.C. grants to Professor R. J. Berry and Dr. H. Kacser, whom we should also like to thank for much help and useful discussion.     

The genetics of glutamic-pyruvic transaminase in mice: Inheritance,electrophoretic phenotypes,and postnatal changes

Glutamic-pyruvic transaminase (GPT, E.C. 2.6.1.2) from 18 inbred strains of mice was subjected to starch gel electrophoresis. Two electrophoretic phenotypes were observed: a fast-migrating pattern in 16 strains and a slower-migrating pattern in two strains. A comparison of electrophoretic patterns of F₁ and backcross progeny of two strains of mice showed that the inheritance of GPT is autosomal with two codominant alleles. The genetic locus for GPT is designated Gpt-1, and its two alleles are designated Gpt-1 ^a and Gpt-1 ^b to represent the fast-migrating (A) and slow-migrating (B) patterns. The GPT was expressed in 11 tissues with different amounts of enzyme activity. Developmental studies of GPT activity in liver showed that between 5 and 12 days after birth the mean activity was 10 units/g protein. Between 12 and 19 days, a dramatic rise in activity occurred and adult values of 300 units/g protein were reached by 26 days.This research was supported by The National Foundation (CRBS-258) and the National Institutes of Health (GM15253).Preliminary results were reported at the Annual Meeting of the American Society of Human Genetics, October 11–14, 1972, in Philadelphia.R. P. D. is an investigator of the Howard Hughes Medical Institute.     

Phosphoglucomutase electrophoretic variants in the mouse

The phosphoglucomutase (PGM) electrophoretic phenotype of the mouse (Mus musculus) consists of several distinct components which can be grouped into two major zones designated PGM-1 and PGM-2. Evidence presented here indicates that each zone is controlled by a single genetic locus denoted Pgm-1 and Pgm-2, respectively. Two variant forms segregated at the Pgm-1 locus. They were codominantly expressed and inherited as alleles at an autosomal locus. The alleles were termed Pgm-1 ^a (fast) and Pgm-1 ^b (slow). These alleles were separately fixed in a number of inbred strains of mice. Preliminary evidence based on wild mouse phenotypes indicates that variant forms also exist for PGM-2 which are inherited as alleles at an autosomal locus. Genetic linkage relationships have not been determined for these loci. PGM-1 variants and PGM-2 were expressed in mouse fibroblasts in vitro.Supported by U.S. Public Health Service grants GM-09966 and GM-07249 from General Medical Sciences and 5 F2 HD-35,531 from Child Health and Human Development; and Atomic Energy Commission contract AT(30-1)-3671.Postdoctoral Fellow of the U.S. Public Health Service.     

Genetic studies of murine catalase: Regulation of multiple molecular forms of kidney catalase

Starch gel electrophoresis of kidney catalase in inbred strains C3H and C57BL/6, their F₁ hybrid, and first and second backcross generations demonstrated that single-component (type A) v. multiple-component (type B) electrophoretic patterns are controlled by a single locus. The type A electrophoretic pattern is dominant. Twenty-five inbred strains of mice were classified according to their kidney catalase electrophoretic pattern. The data indicate that the segregating genetic factor determines a specific substance in the type A kidney which affects the electrophoretic mobility of catalase. A comparison of the F₁ hybrid enzyme with a 1:1 mixture of C3H and C57BL/6 enzyme showed that the alteration of electrophoretic mobility is the result of posttranslational modification of the catalase molecule. An association of kidney catalase electrophoretic pattern and the H-2 ^k haplotype indicates that the locus controlling the electrophoretic pattern is most likely located on chromosome 17 in close proximity to the H-2 complex.     

Glucose phosphate isomerase enzyme-activity mutants inMus musculus: Genetical and biochemical characterization

Two glucose-6-phosphate isomerase (GPI) mutants with approximately 60% residual activity in blood compared to wild type have been independently detected in offspring derived from 1-ethyl-1-nitrosourea-treated male mice. Homozygous mutants with about 20% residual activity were recovered in progeny of inter se matings of heterozygotes. However, in both mutant lines the number of homozygous mutants was less than expected suggesting an increased lethality of these animals. Results of linkage studies and of investigations of physicochemical properties of the mutant enzymes indicate point mutations at theGpi-1s structural locus on chromosome 7. Based on these findings the two new alleles were designatedGpi-1s ^b-m1Neu andGpi-1s ^b-m2Neu, respectively. The b-m1Neu allele codes for an erythrocyte enzyme which, in the homodimeric form, exhibits a decreased stability toward heat and urea, an altered isoelectric point, normalpH dependence, an increasedK _m for fructose-6-phosphate, and increasedK _i's for 6-phosphogluconate and 2,3-diphosphoglycerate (2,3-DPG) compared to the wild-type enzyme. The GPI-1s^b-m2Neu homodimer, in contrast, is characterized by an even stronger instability, slightly alteredpH dependence, an increasedK _i for 2,3-DPG, normal other kinetics, and normal isoelectric point. The different degree of stability of the mutant homodimersin vitro seems to be reflected in a different degree of stabilityin vivo, since GPI deficiency in general is more strongly expressed in the tissues of the homozygousGpi-1s ^b-m2Neu mutant compared to the homozygousGpi-1s ^b-m1Neu mutant. The similarity of the mutant enzymes to the allozymes found in human GPI deficiencies indicates the GPI deficient mouse mutants to be excellent models for the human disease.This research was supported in part by Contract BI6-156-D from the Commission of the European Communities.     

Genetic control of the quantitative variation of erythrocytic glyoxalase-1 (GLO-1) in mice

Quantitative genetic variation in the glyoxalase-1 content (QGlo-1) of red cells of mice is described. Its genetic control is shown to be exerted by either the Glo-1 locus or a closely linked gene to the left of H-2K. At least six alleles, designated QGlo-1 ^a through QGlo-1 ^f, can be found in different inbred strains of mice.This work was supported in part by Grants HL 0911 and AI 15413 of the National Institutes of Health and by a grant from the Sally and Alma Solomon Foundation.     

Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse: Evidence for a cis-acting regulator gene (Adt-1) controlling C2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adt-1 on chromsome 3

An electrophoretic variant previously reported for the stomach isozyme of alcohol dehydrogenase (ADH-C2) in inbred strains of Mus musculus (Holmes, 1977) has been used to localize the gene encoding this enzyme (Adh-3) on chromosome 3 near Va (varitint) (9.6 ± 3.6% recombinants). Genetic variation of ADH-C2 activity in male and female reproductive tissues among inbred strains and Harwell linkage testing stocks was also observed. Reproductive tissue ADH-C2 phenotypes were inherited in a normal Mendelian fashion among F₂ progeny of an F₁ (LII × C57BL/Go) × C57BL/Go backcross as though controlled by a single cis-acting regulator locus (designated Adt-1) with two alleles: Adt-1 ^a (presence of ADH-C2) and Adt-1 ^b (absence or low activity of ADH-C2). No recombinants were observed among 73 progeny or among 13 inbred strains and six Harwell linkage testing stocks of mice, indicating that Adh-3 and Adt-1 are closely linked or identical genes. A single recombinant phenotype was observed in Peru-Coppock mice, suggesting that they are separate genes. Ontogenetic analyses demonstrated that ADH-B₂ is present throughout development from late fetal stages in stomach, liver, and kidney; similar results were found for ADH-C2 in developing kidney and stomach extracts, whereas ADH-A2 exhibited high activity in liver extracts after 3 weeks of age in both sexes and in male kidney extracts after 6 weeks.     

Mouse aldehyde dehydrogenase genetics: Positioning of Ahd-1 on chromosome 4

Electrophoretic variants of mitochondrial aldehyde dehydrogenase (AHD-A₂) are widely distributed among inbred strains of Mus musculus and have been used to localize the gene encoding AHD-A₂(Ahd-1) at the non-centromeric end of chromosome 4. In the mouse (Mus musculus), aldehyde dehydrogenase (AHD; E.C.1.2.1.3) exists as at least three isozymes which are differentially distributed in liver subcellular fractions (designated A₂, B₄ and Cy* for the mitochondrial, soluble and microsomal isozymes respectively) and in various tissues of this animal (Holmes, 1978a; 1978b; Timms & Holmes, 1981). Electrophoretic variants have been previously reported for the A₂ and B₄ isozymes among inbred strains of mice, and the genetic loci (designated Ahd-1 and Ahd-2) have been localized on chromosomes 4 and 19 respectively (Holmes, 1978b; Timms & Holmes, 1980). This paper describes further genetic analyses of AHD-A₂ enabling Ahd-1 to be positioned at the non-centromeric end of chromosome 4. Forty-three inbred strains of Mus musculus were used in these studies (Table 1). Two series of matings were carried out. 1) Female SM/J mice and male NZC/B1 mice were mated to obtain F, female offspring which were backcrossed to male NZC/B1 mice. These progeny were used to examine the segregation and linkage relationship of b (brown), Pgm-2 (encoding phosphoglucomutase B) and Ahd-1 (Table 2). 2) Female C57BL/6J mice and male SM/J. mice were mated to obtain F, female offspring which were backcrossed to male SM/J mice. The segregation and linkage relationship of Pgm-2, Gpd-1 (encoding the liver and kidney isozyme of hexose-6 phosphate dehydrogenase) and Ahd-1 were examined for these backcross progeny (Table 3). Methods for preparing liver and kidney extracts and the cellulose acetate electrophoresis procedure for typing Ahd-1, Pgm-2 and Gpd-1 have been previously described (Holmes, 1978b). A previous study has described the electrophoretic patterns for allelic variants for mitochondria1 AHD and of the hybrid phenotype for this enzyme (Holmes, 1978b). The three-allelic isozyme pattern for hybrid animals was consistent with a dimeric subunit structure: AHD-A¹A², AHD-A¹A² and AHD-3, with the A1 and A2 subunits being encoded by separate alleles at a single locus, designated Ahd-1 (Ahd-1^oand Ahd-1^brespectively). The distribution of these alleles among 43 inbred strains of mice is given in Table 1. The allelic variants were approximately equally distributed among the inbred strains examined and no divergence of phenotype was observed among the 6 substrains of C57BL mice (Ahd-1^aallele) and 5 substrains of BALB/c (Ahd-1^ballele) mice examined. Genetic variants for phosphoglucomutase-B (PGM-B) have been reported by Shows, Ruddle and Roderick (1969) and the gene (Pgm-2) was subsequently localized on chromosome 4 near b (brown) by Chapman, Ruddle and Roderick (1970). Table 2 illustrates the results of a three-point cross between b, Pgm-2 and Ahd-1. Variation from the expected 1:1:1:1:1:1 ratio for unlinked loci was significant(x²= 73.15; 7 df; P < 1 × 10^-5), indicating that the three loci are linked. Recombination frequency data are consistent with the gene order: b - Pgm-2 - Ahd-1 The second cross examined the segregation of Pgm-2, Ahd-1 and Gpd-1 loci (Table 3). The latter locus has been previously positioned on chromosome 4 (linkage group VIII) by Hutton & Roderick (1970) and Chapman (1975), and has been used to localize Ahd-1 in this region (Ahd-1 and Gpd-1 exhibit a recombination frequency of 10.3 ± 3.7 %) (Holmes, 1978b). The data from Table 3 is consistent with a gene order of Pgm-2 - Ahd-1 - Gpd-1. The recombination frequency data of Ahd-1 with Gpd-1, Pgm-2 and b also supports the proposal that Ahd-1 is localized between Pgm-2 and Gpd-1 (Tables 2 and 3; Holmes, 1978b). Recent metabolic studies have indicated that mitochondria1 aldehyde dehydrogenase (AHD) plays a very important role in the metabolism of acetaldehyde derived from ethanol, ensuring a low concentration of acetaldehyde in the blood leaving the liver (Grunnet, 1973; Parilla et al., 1974; Corral1 et al., 1976). Moreover, genetic variation of this isozyme in human livers has been recently reported (Harada et al., 1978), and this polymorphism has been proposed as the molecular basis for individual and racial differences in alcohol sensitivity (Goedde et al., 1979). Consequently, genetic analyses of mitochondria1 AHD are of particular significance to studies on the genetic control of alcohol metabolism in mammals. In summary, this report confirms previous studies which demonstrated that the genetic locus encoding mitochondrial aldehyde dehydrogenase in the mouse (Ahd-1) is on chromosome 4 (Holmes, 1978b), and positions the gene with respect to b (brown), Pgrn-2 (encoding phosphoglucomutase B) and Gpd-1 (encoding the liver and kidney isozyme of hexose-6-phosphate dehydrogenase). In addition, the distribution of the 2-allelic phenotypes for this isozyme has been examined among 43 in- bred strains of mice.     

Electrophoretic heterogeneity of mouse erythrocyte peptidases

Starch gel electrophoresis in conjunction with a specific staining method revealed the occurrence of five distinct peptidases in mouse red blood cells. These enzymes can be distinguished on the basis of substrate specificity and electrophoretic mobility. They have been designated peptidases A, B, C, D, and E to correspond with the nomenclature adopted for human peptidases with which the mouse enzymes appear to be homologous. Genetically determined variants of peptidase C are described. The phenotype Pep C1 occurs in C57BL/Gr mice and the phenotype Pep C2 in CBA/Gr and Strong A/Gr mice. These phenotypes and the presumed heterozygote, Pep C2-1, appear to be due to the occurrence of codominant autosomal alleles which have been designated Pep-C ¹ and Pep-C ². F₁ and F₂ crosses show segregation in the expected Mendelian ratios. F₂ embryos and their placentae show the same electrophoretic pattern for peptidase C. The occurrence of a separate locus controlling the structure of each distinct peptidase is postulated.     

Genetics of an esterase in Aedes aegypti

Zymograms of single individuals of Aedes aegypti were obtained by means of starch gel electrophoresis, using alpha-naphthyl acetate as substrate. Inbred lines gave consistently homogeneous patterns; earlier results from random-breeding laboratory strains had shown considerable variability. Six distinct bands were observed. The furthest moving band, designated Esterase 6, showed differential migration in two inbred lines. Reciprocal crosses between these lines gave F₁ progeny showing both bands. Backcrosses of F₁ to either parental line gave a 1:1 segregation. These results are consistent with the hypothesis that the two forms of Esterase 6 are controlled by a single pair of codominant alleles at a single gene locus (Est 6 ^a and Est 6 ^b). Linkage tests with marker genes have demonstrated that Est 6 is on linkage group 2, with the following alignment: spot-abdomen (9.0±1.0) yellow-larva (17.4±1.3) Est 6. Crosses with another inbred line demonstrated a third band with intermediate mobility, designated Est 6 ^c. An additional electrophoretic variant which seems to have a simple Mendelian basis was found in esterase band 1.This work was supported by NIH Research Grant No. A1-02753.     

Allelic forms of mouse transcobalamin 2

Transcobalamin 2 is the only vitamin B12-binding protein found in mouse serum. Two allelic forms of mouse transcobalamin 2 are described. The two forms differ in their mobilities on polyacrylamide gel electrophoresis. The slowly migrating form has been found in serum from 25 inbred mouse strains. The more rapidly migrating form was detected in 3 inbred mouse strains (NZB, ST/bJ, and CPB-WV). Both parental variants were expressed in F₁ progeny of appropriate interstrain crosses, showing codominant expression of the transcobalamin 2 alleles. In backcrosses between F₁ and parental individuals, the two electrophoretic variants were inherited as single Mendelian traits. The strain distribution pattern of the two variants in recombinant inbred lines likewise suggested a single-gene mode of inheritance and indicated a lack of close linkage with a number of genetic loci on chromosomes 1, 2, 4, 5, 6, 7, 9, 12, 14, 15, and 17. We propose the symbol Tcn-2 for the polymorphic gene locus coding for transcobalamin 2 in the mouse and Tcn-2 ^s and Tcn-2 ^f for the two alleles.     

Esterase-8 (Es-8): Characterization,polymorphism, and linkage of an erythrocyte esterase locus on chromosome 7 of Mus musculus

An electrophoretic polymorphism of an erythrocyte esterase, esterase-8, specific for the substrates α- and β-naphthyl acetate has been observed in the Asian house mouse, Mus musculus castaneus. M. m. castaneus is interfertile with inbred strains of mice, and F₁ hybrids (C57BL/6J × castaneus)F₁ and (SWR/J × castaneus)F₁ show a double-banded phenotype similar to a mixture of parental forms. This pattern suggests codominant expression of a structural gene difference. In backcrosses, ES-8 segregated as a single autosomal gene, designated Es-8, linked to Gpi-1 on chromosome 7. A gene order of Es-8, Gpi-1, c, Mod-2, and Hbb was determined from a series of crosses.     

A serum protein polymorphism determinant on chromosome 9 of Mus musculus

Summary Genetic polymorphism for a previously undescribed serum protein has been found among inbred strains of Mus musculus. The new serum protein locus, gene symbol Sep-1, has been located on Chromosome 9, gene order Lap-1-Sep-1-Mpi-1-d-Mod-1, by utilizing information obtained from 52 recombinant inbred strains together with standard genetic backcrosses. The strain distribution pattern for this locus, supernatant malic enzyme, and transferrin, also on Chromosome 9, are given for 67 inbred strains. Because the genotype of SEP-1 can be determined for individual mice without killing them, Sep-1 is a very useful gene in linkage studies and experimental biology.     

Genetics of ocular NAD+-dependent alcohol dehydrogenase and aldehyde dehydrogenase in the mouse: Evidence for genetic identity with stomach isozymes and localization ofAhd-4 on chromosome 11 near trembler

Electrophoretic and activity variation of the stomach and ocular isozyme of aldehyde dehydrogenase (designated AHD-4) was observed between C57BL/6J and SWR/J inbred strains of mice. The phenotypes were inherited in a normal mendelian fashion, with two alleles at a single locus (Ahd-4) showing codominant expression. The alleles assorted independently of those atAdh-3 [encoding the stomach and ocular isozyme of alcohol dehydrogenase (ADH-C₂)] on chromosome 3. Three chromosome 11 markers, hemoglobin -chain (Hba), trembler (Tr), and rex (Re), were used in backcross analyses which established thatAhd-4 is closely linked to trembler. The distribution patterns for stomach and ocular AHD-4 phenotypes were examined among SWXL recombinant inbred mice, and those for stomach and ocular ADH-C₂ among BXD recombinant inbred strains. The data provided evidence for the genetic identity of stomach and ocular ADH-C₂ and of stomach and ocular AHD-4.This research was supported in part by the U.S. Department of Energy under Contract DE-ACO5-84OR214000 with Martin Marietta Energy Systems, Inc. (to R.A.P.).     

Chromosomal location of the gene encoding the murine acute-phase protein serum amyloid P-component (SAP)

A full-length cDNA clone, pmSAP3, encoding the serum P component (SAP), has been used to search for DNA fragment length variation among mouse strains previously analyzed for differences in endogenous SAP levels. Three alleles were found usingEcoRI-digested DNA. The finding of a single 5.4-kb fragment, alleled, in DNA from DBA/2J mice suggests the presence of a singleSap locus. Segregation of DNA fragment associated withSap ^b andSap ^d alleles was analyzed in three sets of recombinant inbred (RI) strains. The strain distribution pattern found for theSap alleles was identical to that of alleles ofLy-9 in 43 individual RI strains, suggesting tight linkage withLy-9 on mouse chromosome 1. In the BXD RI strains, the SDP of theSap locus, defined by the difference in the endogenous SAP level, is also identical to the SDP of the DNA fragments. We propose to redesignate theSap locus to include both the structural element defined by the DNA polymorphism and the regulatory element involved in the regulation of SAP synthesis. TheSap locus is the major genetic element contributing to the regulation of SAP production. Other genetic factors are also involved, as shown by the presence of nonparental phenotypes in the individual BXH RI strains. This study was performed through special Coordination Funds of the Science and Technology Agency of the Japanese Government and PHS Grant GM24464 to R.W.E.     

An acid phosphatase locus expressed in mouse kidney (Apk) and its genetic location on chromosome 10

A genetic locus controlling the electrophoretic mobility of an acid phosphatase in mouse kidney is described. This locus, called acid phosphatase-kidney (Apk), is not expressed in erythrocytes, liver, spleen, heart, lung, brain, skeletal muscle, stomach, or testes. The product of Apk hydrolyzes the substrate naphthol AS-MX phosphoric acid but is not active on a-naphthylphosphate or 4-methylumbelliferylphosphate. It is not inactivated by 50 C for 1 hr, nor is its electrophoretic mobility altered by incubation with neuraminidase. The locus is invariant among 31 inbred strains (Apk ^a), with a variant allele (Apk ^m) observed only in Mus musculus molossinus. Codominant expression was observed in F₁ hybrids of M. m. molossinus and inbred strains. Apk was mapped on Chr 10, near the neurological mutant waltzer (v).This work was supported by Contract NO1-ES42159 from the National Institute of Environmental Health Sciences and by Grant 1-476 from the National Foundation—March of Dimes. The Jackson Laboratory is fully accredited by the American Association for Accreditation of Laboratory Animal Care.     

Genetic analysis of human lymphocyte proteins by two-dimensional gel electrophoresis: 4. Genetic polymorphism of cytosol 100k polypeptide

Summary We describe a genetic polymorphism of a human cellular polypeptide with mol. wt. 100,000, detected in peripheral blood lymphocytes by high resolution two-dimensional electrophoresis. Three different electrophoretic types (1-1, 2-1, and 2-2) of the polypeptide have been identified. Family and population studies indicate that the three phenotypes of the polypeptide are determined by two common alleles at a single autosomal locus. The polypeptide occurs in the cytosol and is one of the abundant polypeptides of B-lymphoblastoid cells, T-lymphoblastoid cells, fibroblasts, and HeLa cells. The data indicate that the cytosol polypeptide with mol.wt. 100,000 shows a genetic polymorphism determined by aew autosomal locus. It is proposed that the polypeptide and its locus be temporarily designated cytosol 100k polypeptide (C100k polypeptide) and C100P, respectively. In a Japanese population, the gene frequencies of C100P ¹ and C100P ² were 0.907 and 0.093, respectively.     

Phosphoglucomutase isozymes of red cells in Mus musculus: Additional polymorphism at PGM-1 compared by two electrophoretic systems

Phosphoglucomutase (PGM) of red cells was examined in 15 inbred strains of mice, using two different starch gel electrophoretic buffer systems. Two new alleles, Pgm-1 ^c and Pgm-1 ^d, were discovered at the Pgm-1 locus. Pgm-1 ^c was first identified in strain C3H/HeNWe and Pgm-1 ^d in 129/ReWl. No variation was observed at the Pgm-2 locus.Supported in part by USPHS Pre-doctoral Fellowship No. 5 F1 GM-32,680, USPHS Research Resources Grant No. 5-PO6 RR 00343-05, USPHS (National Cancer Institute) Chemotherapy Contract 71-2010, and Biomedical Sciences Support Grant FR 07037 to the University of Kansas.