Genetic variants of hemoglobin in canine erythrocytes*

Genetic polymorphism of hemoglobin was found in the erythrocytes of dogs of seven Japanese native breeds by using starch gel electrophoresis. Analysis of parentage records of the dogs revealed that the phenotypic variation of hemoglobin is controlled by one autosomal locus with two codominant alleles, Hb^A and Hb^B. The allele Hb^A occurred only in Japanese native breeds except Shikoku. The frequency of Hb^A in the Japanese breeds was low and 0.08. All the dogs belonging to 25 European breeds and 5 oriental origin (except Japan) breeds examined in this experiments had the homozygous genotype constitution Hb^B/Hb^B.     

Phosphohexose isomerase polymorphism in horse erythrocytes

Four individual patterns of phosphohexose isomerase (PHI) from horse red cells were found by starch gel electrophoresis. Population and family data of two Swedish horse breeds were consistent with the theory that the PHI types were controlled by three codominant, autosomal alleles designated PHI^F, PHI^I and PHI^S( F , I and S ).     

Electrophoretic types of leucine aminopeptidase in sheep serum

Leucine aminopeptidase in sheep serum was studied by starch gel electrophoresis. Two phenotypes, A and B, were observed, of which the former was present in 70–90 % of all the sheep examined. These two phenotypes have been shown to be controlled by a single autosomal locus, with two alleles Lay^A and Lap^B . The Lap^A allele is dominant. The frequencies of Lap phenotypes and alleles were determined in eleven Spanish and two foreign breeds. Serum alkaline phospatase and serum leucine aminopeptidase are electrophoretically distinct.     

Genetic polymorphism of erythrocyte esterase-D in pigs

The erythrocyte esterase-D (Es-D) of four European-American pig breeds, two Taiwan native pigs (Taoyuan and Short ear breeds), Philippine native pig and wild boar populations (Sus scrofa riukiuanus) in Japan was investigated by using starch gel electrophoresis. Analysis of parentage records of the pigs revealed that the phenotypic variation of erythrocyte esterase-D was controlled by two codomi-nant alleles Es-D^A and Es-D^B. The allele Es-D^b was mostly found in three European -American pig breeds, Landrace (0.100), Hampshire (0.135) and Duroc (0.102). All of the wild boar populations were monomorphic for allele Es-D^A.     

Polymorphism of red cell acid phosphatase in dogs

In fresh red cell haemolysates from Labrador retriever dogs three acid phosphatase (Pac) phenotypes were found by starch gel electrophoresis. Family data were consistent with the theory that the Pac phenotypes are controlled by two codominant, autosomal alleles, designated Pac ^F and Pac ^S.     

Polymorphism in glucose-6-phosphate dehydrogenase in the German Large-White

Glucose-6-phosphate dehydrogenase was tested in haemolysed swine erythrocytes by starch gel electrophoresis. In the German Large-White this system is genetically controlled by two alleles, G-6-PD ^A and G-6-PD ^B.     

Polymorphism of postalbumins in the serum of pigs and the ovarian follicular fluid of sows

By means of starch-gel electrophoresis blood serum postalbumins of pigs were separated into two polymorphic regions. The first region forms a genetic system determined by two codominant alleles, Pa ₁^A and PA ₁^B. Segregation data are presented which support this hypothesis. It was found that neither sex nor age of the animal have any influence on the mobility of fractions. Identical types of blood serum postalbumins were also found in the ovarian follicle fluid.     

Phosphohexose isomerase polymorphism in the domestic cat

Genetic variation of the enzyme phosphohexose isomerase (PHI) has been found in the erythrocytes of Australian domestic cats by horizontal starch gel electrophoresis at pH 8.2. Three complex patterns of isoenzymes, designated F, FS and S, were obtained migrating anodally. Limited family studies and the distribution of the three main phenotypes indicated that the polymorphism is controlled by two codominant autosomal alleles, PHI^F and PHI^S Gene frequencies for PHI^F and PHI^S have been calculated as 0.036 and 0.964 respectively. Three additional variant forms have also been observed.     

Equine markers genes. Polymorphism for group-specific component (Gc)

Polymorphism of equine Gc protein was demonstrated by immunofixation electrophoresis with a goat anti-human Gc antibody. Three different phenotypes, F, FS and S, were found. Family data supported the genetic theory of two autosomal co-dominant alleles, Gc^F and Gc^S. Both alleles occurred in Standardbred, Thoroughbred and Arabian horses and in Shetland ponies. A frequency of 0.23 for Gc^S in the American Standardbred horse indicates the system should be useful for problems of identification and parentage.     

Genetic variants of phosvitin in egg yolk of the Japanese quail, Coturnix coturnix japonica

Summary. Phosvitin polymorphism in egg yolk of the Japanese quail was found by horizontal polyacrylamide gradient gel electrophoresis. Six phenotypes of yolk phosvitin designated A, B, C, AB, AC, and BC were observed in a population of 281 birds. Analysis of family data revealed that the phenotypic variation of quail yolk phosvitins was controlled by an autosomal Pv locus with three codominant alleles, Pv^a, Pv^b and Pv^c. The gene frequencies of Pv^a, Pv^b and Pv^c were 0.064, 0.824 and 0.112, respectively.     

Inheritance of adenosine deaminase variants in chickens and turkeys

Blood cell lysates of chickens and turkeys were subjected to starch gel electrophoresis and the gels were stained for adenosine deaminase. Two zones were observed singly or together in the electrophoretic patterns of each lysate. Zones of chicken lysates were analogous in electrophoretic mobility to those of turkeys. An extra zone which appeared in patterns of a sample stored over one month was not detected in patterns of a second aliquot of stored sample treated with a reducing agent prior to electrophoresis.
Family data involving 110 chicken progeny and 221 turkey progeny supported the hypothesis that these zones were controlled by two codominant alleles designated ADA.⁴ and ADA^B. In the two Leghorn strains studied ADA^B was much more frequent than ADA.⁴, but the frequency distribution was reversed in the Small White turkey strain examined.     

Partial purification and some biochemical properties of nonspecific alkaline phosphatase in germinating chick-pea (Cicer arietinum) seeds

A procedure for the partial purification of a non-specific alkaline phosphatase (EC 3.1.3.1.) from the embryonic axes of chick-pea seeds is described. Ammonium sulphate precipitation, DEAE-cellulase chromatography, Sephacryl S-200 chroma-tography and polyacrylamide gel electrophoresis are the most important steps. The molecular weight of this non-specific enzyme, as determined by Sephacryl S–200 gel filtration and SDS–polyacrylamide gel electrophoresis, was estimated as being 68 and 78 kDa respectively; the optimum pH for p-nitrophenylphosphate hydrolysis was 7.5, and the K_m for this artificial substrate was 0.5 mM. The enzyme catalyzes the hydrolysis of a variety of organic phosphate esters. The best substrates are: phos-phoenolpymvate (K_m= 2.4 m M ), NADP⁺ (K_m= 4.0 m M ), 5'-AMP (K_m= 4.5 m M ), 5'-ADP (K_m= 6.1 m M ) and ribose-5P (K_m= 5.8 m M ); but it is unable to hydrolyze 5'-ATP, phosphocreatine and tripolyphosptiate. Phospate was a competitive inhibitor. Zn²⁺, K⁺, Hg²⁺ and Mo⁶⁺ were strong inhibitors, whereas F⁻ and Ca²⁺ inhibited weakly; Co²⁺ and Ni²⁺ were activators.     

Genetical control of phosphoglucose isomerase isozymes in the Japanese quail erythrocytes

Three phenotypes of phosphoglucose isomerase (PGI) from the Japanese quail erythrocytes were observed by horizontal starch gel electrophoresis. Population and family data from one laboratory population of quail was consistent with the theory that PGI polymorphism was controlled by two codominant, autosomal alleles designated PGI^F and PGI^S with gene frequency values 0.25 and 0.75, respectively. The study supported the earlier view that the Japanese quail is highly polymorphic with regard to biochemical variation.     

A transferrin variant Tf I in crosses of the wild and domestic pigs

In crosses of the wild pig (Sus scrofa attila Thomas) with the domestic pig a transferrin variant, Tf I, was detected, electrophoretic mobility of which was slightly faster than the mobility of the variant Tf A. From the results of starch gel electrophoresis, isolation, neuraminidase treatment, autoradiography, and genetic analysis of several families, it can be concluded that the Tf I variant is genetically controlled by the allele Tf¹. Thus the number of alleles in the transferrin system of the pig has increased to six ( Tf^I, Tf^ATf^B, Tf^C, TP^D and Tf^E ).     

Variation of acidic prealbumins in the donkey (Equus asinus)

Starch gel electrophoresis of 55 donkey serum samples revealed three prealbumin (Pr) phenotypes temporarily designated PrM, PrMT and PrT. The distribution was in agreement with a genetic theory of two codominant alleles of frequencies, Pr^M= 0.87 and Pr^T= 0.13. Variation was also observed for proteins migrating with the same rate as the Xh zones in the horse.     

Plasma esterase polymorphism in the Bank vole, Clethrionomys glareolus, in Britain

Three hundred and eighty-three Clethrionomys glareolus from 20 localities in England, Wales and Scotland were typed for plasma esterase and a genetic polymorphism was discovered. The esterase was named Es-1. Breeding tests suggested that three alleles were segregating: Es-1^o when homozygous results in complete absence of enzyme activity. The active alleles Es-1^f and Es-1^s code for enzyme variants which migrate more rapidly and less rapidly, respectively, under starch gel electrophoresis. Of these active alleles, Es-1^f is morc common in the north of Britain and Es-1⁸ in the south. A 23-month field study on two areas at Wicken Fen, Cambridgeshire, suggested that animals possessing Es-1^s survived less well at high population densities, perhaps through their being more likely to emigrate.     

Purification of an α-L-arabinofuranosidase from carrot cell cultures and its involvement in arabinose-rich polymer degradation

Konno, H., Yamasaki, Y. and Katoh, K. 1987. Purification of an α-L-arabinofurano-sidase from carrot cell cultures and its involvement in arabinose-rich polymer degradation.
An α-L-arabinofuranosidase (α-L-arabinofuranoside arabinofuranohydrolase, EC 3.2.1.55) was isolated from a homogenate of cell suspension cultures of carrot ( Daucus carota L. cv. Kintoki). The buffer-soluble enzyme was purified to homogeneity by a procedure involving ammonium sulfate fractionation, chromatography on DEAE-Sephadex A-50, Sephadex G-150, Con A-Sepharose 4B and CM-Sephadex C-50, and preparative polyacrylamide gel electrophoresis. The size of this enzyme as determined by polyacrylamide gel electrophoresis in the presence of sodium laurylsulfate and by Sephadex G-200 gel filtration was 94 and 110 kDa, respectively. The isoelectric point was at pH 4.7. The K_m and V_max values for p-nitrophenyl α-L-arabinofuranoside were 1.33 mM and 20.2 μimol (mg protein)^-1 h^-1, respectively. The optimal activity occurred at pH 4.2 with Mcllvaine buffer. The enzyme was stimulated by Ca²⁺ and Zn²⁺, whereas it was strongly inhibited by Cu²⁺, Ag²⁺, Hg²⁺, p-chloromercuri-benzoate and L-arabono-l,4-lactone. The enzyme acted on beet arabinan in an exo-fashion. Furthermore, the enzyme was partially involved in the hydrolysis of the ara-binogalactan and pectic polymer purified from carrot cell walls.     

Serum albumin polymorphism and its relationship to economic traits in crossbred cattle

The serum albumin genotypes of 65 Jersey × Hariana (F₁), 75 Holstein Friesian × Hariana (F₁) and 47 Brown Swiss × Hariana (F₁) crossbred cows were determined by starch gel electrophoresis. Two albumin alleles Alb^F and Alb^s , but only either as Alb^F homozygotes or Alb^Fs heterozygotes, were observed amongst these animals. There were no Alb^S homozygotes or other genotypes. Highly significant relationships between albumin genotypes and both birth weights and first-lactation milk yields of these cows were observed. The Alb^F allele was associated with increased milk yield and greater birth weights.     

Purification and characterization of a streptomycete collagenase

A soil streptomycete designated as Streptomyces sp. A₈ produced an extracellular collagen hydrolysing enzyme that appeared to be 'true collagenase'as it degraded native collagen under physiological conditions and cleaved the synthetic hexapeptide 4-phenylazobenzyloxycarbonyl-L-prolyl-L-leucyl-glycyl-L-prolyl-D-arginine into two tripeptides. The enzyme was purified by diethyl aminoethyl cellulose chromatography and Sephadex G-150 gel filtration. The purified enzyme had an apparent molecular weight of about 75000 by SDS-polyacrylamide gel electrophoresis. Treatment with lithium chloride did not dissociate it into subunits. A strong inhibition was observed with chelating agents such as α-α-dipyridyl and 8-hydroxyquinoline. Ethylene diamine tetracetate completely inhibited the enzyme activity. Among the cations tested only Ca^{2 +} and Mg^{2 +} enhanced the collagenase activity. Heavy metal ions like Pb^{2 +}, Ag⁺, Cu^{2 +} and Zn^{2 +} strongly inhibited the enzyme. The EDTA inhibition could be reversed with Ca^{2 +}. Cysteine and reduced glutathione caused significant reduction in enzyme activity. Parachloromercuribenzoate and iodoacetamide had no effect on the collagenase. Amino acid analysis revealed the absence of cysteine and tyrosine. Many of the properties were the same as collagenases of Clostridium histolyticum and Vibrio alginolyticus.     

Isolation and characterization of large lactococcal phage resistance plasmids by pulsed-field gel electrophoresis

Abstract Five phage-resistant Lactococcus lactis strains were able to transfer by conjugation the lactose-fermenting ability (Lac⁺) to a plasmid-free Lac⁻ L. lactis strain. In each case, some Lac⁺ transconjugants were phage-resistant and contained one or two additional plasmids of high molecular mass, as demonstrated by pulsed-field gel electrophoresis. Plasmids pPF144 (144 kb), pPF107 (107 kb), pPF118 (118 kb), pPF72 (72 kb) and pPF66 (66 kb) were characterized: they are conjugative (Tra⁺), they confer a phage-resistant phenotype and they bear lactose-fermenting ability (Lactose plasmid) except for the last two. Plasmids pPF144, pPF107 and pPF118 resulted probably from a cointegrate formation between the Lactose plasmid and another plasmid of the donor strain, whereas pPF72, pPF66 and the Lactose plasmid were distinct in the corresponding transconjugants. Plasmids pPF72 and pPF66 produced a bacteriocin. At 30°C, the phage resistance conferred by the plasmids was complete against small isometric-headed phage and partial against prolate-headed phage, except for pPF107 whose phage resistance mechanism was totally effective against both types of phages, but was completely inactivated at 40°C. Restriction maps of four of the plasmids were constructed using pulsed-field gel electrophoresis.