On the phenotype distribution of red cell acid phosphatase in Czechoslovakia

Summary A random group of 300 donors living in the district of eské Budjovice (southern Bohemia) have been investigated for the incidence of the individual phenotypes of red cell acid phosphatase. The calculated frequencies of the genes P^a, P^b and P^c are 0.322, 0.615 and 0.063, respectively.     

Isoelectric focusing of human red cell acid phosphatase isozymes

The isoelectric points of human red cell acid phosphatase have been determined by isoelectric focusing. The three homozygous types A, B, and C and the heterozygous type CA have been studied. The isoelectric points of the main isozymes of type A had a higher value than the values found in types B and C. In these two types, the isoelectric points were very similar but the shapes of the elution curves differed. Both the isoelectric points and the shape of the elution curve found in type CA corresponded to a combination of the results found in type A and type C.     

Immunochemical characterization of human red cell acid phosphatase isozymes

An immunological study was performed on human red cell acid phosphatase (ACP1) isozymes encoded by different alleles, each of which is expressed as an electrophoretically fast (f) isozyme and a slow (s) isozyme. These isozymes reacted as two immunochemically different groups. Allele-specific reactions were not detected between either the f isozymes or the s isozymes. Quantitation of ACP1 isozymes in red cells by crossed immunoelectrophoresis revealed a phenotype-dependent variation in the concentration of isozyme protein. A simple gene dosage effect was indicated and the ordering of the ACP1 alleles (ACP1*A < ACP1*B < ACP1*C < ACP1*E) was identical to that found for enzyme activity levels. Also, an allele effect on the proportion between s and f isozymes (s/f) was observed; the ordering here was ACP1* B < ACP1*A < ACP1*, which is the same as that reported for the susceptibility to modulation with purines. These variations in isozyme protein levels appear to account for the phenotypic differences in the intensity of the isozyme bands, when activity-stained after electrophoresis, and in the red cell enzyme activity levels. Investigation of two carriers of a Null allele showed no evidence of an aberrant protein product, and half-normal concentrations of enzyme protein were observed in the red cells of these individuals.     

Human red cell acid phosphatase polymorphism

Red cell acid phosphatase phenotypes were determined in 401 unrelated persons from Southwestern Germany. The frequencies of genes P^a, P^b and P^c were estimated to be p=0.328, q=0.630 and r=0.042.Experiences in 101 cases of disputed paternity with 151 men involved are reported. 22 men could be excluded from paternity on the basis of red cell acid phosphatase phenotypes.In all 140 mother-child-combinations tested the distribution of red cell acid phosphatase variants was compatible with the genetic model suggested by Hopkinson et al.Usefulness of the system in forensic cases of disputed paternity is discussed.Data contained in this paper will also constitute part of the thesis of cand. med. Karl-Henning Lichte.     

The human red cell acid phosphatase activity and its statistical evaluation

Summary We examined 396 bloods samples of the five most common phenotypes of the human red cell acid phosphatase (E.C.3.1.3.2). The different enzyme activity of the individual phenotypes was statistically evaluated and an explanation was sought.     

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.     

Three new phenotypes of human red cell acid phosphatase: ACP1FA,ACP1GA,and ACP1GB

Summary Three new phenotypes of human erythrocyte acid phosphatase (ACP₁) have been detected and found to be unique by direct comparison with previously identified ACP₁ variants. One of these new electrophoretic variants, labeled as ACP₁FA, has been detected in the Hispanic population of California. The electrophoretic variants identified as ACP₁GA and ACP₁GB have been detected in a black family in North Carolina. A family study has shown that ACP ₁ ^G is transmitted as an allele of ACP₁.     

The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3

Human red cell cytosol acid phosphatase activity is supported by a main enzyme which can be extracted by DEAE and phosphocellulose chromatography. It uses pNPP as a substrate and is a protein phosphatase specific to phosphotyrosine. It dephosphorylates the tyrosine-phosphorylated cytosolic fragment of membrane protein 3. When taken together, these results suggest that the physiological role of red cell acid phosphatase is the FB3 phosphotyrosine dephosphorylation. Whatever it may be phosphotyrosine protein phosphatase activity is the first role of red cell acid phosphatase to be demonstrated.     

Some considerations on the geographical distribution of rotifers

In the course of investigations on the systematics and zoogeography of rotifers, the author found that 48% of all taxa treated showed a limited distribution (most were periphytic or benthic periphytic species from shallow waters). The following species were limited to the Palaearctic Region: Marine: Synchaeta triophtalma Lauterborn, S. vorax Rousselet, and S. curvata Lie-Pettersen. Brackish water: Colurella dicentra (Gosse), C. halophila Wulfert, and C. unicauda Eriksen. Among Holarctic species, Notholca psammarina Buchholz & Rühmann and the two semi-species N.(striata) bipalium (O. F. Müller) and N(striata) striata (O. F. Müller) are discussed. A series of warm-stenothermic species were found to be pantropical: Lecane leontina Turner, L. monostyla (Daday), L. harringi (Ahlstrom), Lepadella latusinus (Hilgendorf), Trichocerca chattoni (de Beauchamp), and Platyias leloupi Gillard, while Lecane plesia Myers and L. punctata (Murray) seemed to be confined to the Neotropical Region. The data collected also suggest that:

1. i) Keratella wirketissi Kutikova, K. kamtchatica Kutikova, K. cruciformis (Thompson), and K. eichwaldi (Levander) might be good species.
2. ii) Brachionus forficula Wierzejski, an Old World species, is a geographical vicariant of both B. havanaensis Rousselet and B. trahea Murray from the New World.
3. iii) Cases of ecological vicariance are found in Testidinella elliptica (Ehrb.) and T. clypeata (O. F. Müller) from fresh and brackish water respectively; Keratella cruciformis (Thompson) and K. eichwaldi (Levander) from the sea and brackish water respectively; Keratella quadrata (O. F. Müller), K. valga (Ehrb.), and K. tropica (Apstein), dominant in arctic to cold-moderate, in warm-temperate, and in subtropical-tropical climates respectively.

Some rotifer species are presently in expansion: the cases of K. tropica and of Brachionus falcatus Zacharias in Europe are analysed. A related case is that of man-made faunas: the presence of Brachionus havanaensis in Sangchrist Lake, Ill., USA, and the Rotifer fauna of the River Loire (France) are discussed.     

Polymorphism of the red cell acid phosphatase in the Swiss population

Summary The distribution of the red cell acid phosphatase groups was studied on 1365 blood samples of Swiss individuals. The distribution is in agreement with the Hardy-Weinberg equilibrium. Gene frequencies similar to those observed in other Caucasian populations were obtained (P^A=0.345, P^B=0.607, P^C=0.049). In 331 mother/child-combinations, we found no theoretically impossible combinations.     

Phenotypic variation in the phosphotransferase activity of human red cell acid phosphatase (ACP1)

Summary Red cell acid phosphatase (ACP1) catalyses the transfer of phosphate from phosphate ester substrates to suitable acceptor alcohols such as methanol and glycerol. The rate of substrate turnover in the presence of acceptors is increased by the increment of the phosphotransferase reaction, thus allowing this activity to be measured. There is specificity with regard to acceptors: (a) polyols (e.g., glycerol) are better acceptors than the corresponding n-alcohols, and (b) polyol configuration and chain length determine acceptor activity. Ribitol was the most efficient acceptor found. Each of the three common ACP1 alleles is represented electrophoretically by two isozyme bands; the phosphotransferase activity of the anodal isozyme was found to be more than twice that of the cathodal isozyme. The extent of phosphotransferase activity is also genotype dependent. In the presence of 2M glycerol, the relative phosphotransferase efficiencies for the three homozygote types were: ACP1^*B=3.7, ACP1^*A=3.4, and ACP1^*C =2.5. This pattern of B>A>C is the same as found for the modulation of ACP1 by purines and folates.Publication no. 278 of the Forensic Science Group, School of Public Health, University of California