Peptidases A, B, C, D and S in the American mink: polymorphism and chromosome localization.

An electrophoretic analysis of peptidases was carried out in a population of American mink. Based on substrate and tissue specificities, as well as subunit composition, homologies were established between mink peptidases A, B, C, D and S and human peptidases. Polymorphism for peptidases B and D was demonstrated for minks of three coat colour types. Breeding data indicated that the peptidase variations are under the control of allele pairs at distinct autosomal loci designated as PEPB and PEPD, respectively. Using a panel of American mink-Chinese hamster hybrid clones, the gene for PEPB was assigned to mink chromosome 9.

An estimation of the degree of the genetic divergence of sibling species Microtus arvalis and Microtus subarvalis (Rodentia) based on electrophoretic analysis.

The electrophoretic mobilities of 52 enzymes and proteins were used as measures of the genetic similarity between the sibling species Microtus arvalis and M. subarvalis. The two vole species differed in the electrophoretic mobilities of seven (glucose-6-phosphate dehydrogenase, adenylate kinase, diaphorase, lactate dehydrogenase-A, alpha-galactosidase, 6-phosphogluconate dehydrogenase, and hemoglobin) of these markers. This allowed us to accept the seven markers assayed as species-specific markers. Based on the frequency distribution of the genes at the polymorphic loci of M. arvalis and M. subarvalis, the degree of their genetic similarity was estimated as 0.312 and the genetic distance as 1.164 by Nei's formula. The estimates for genetic similarity were close to those obtained for species recognized as distinct.

Intracellular mechanisms of the formation of homo- and heteropolymeric isozymes. I. Kinetics of the formation of the heteropolymeric isozyme of malate dehydrogenase in parasexual hybrids of two Acetabularia species.

The isozyme pattern of malate dehydrogenase (MDH) of Acetabularia crenulata and A. mediterranea is characterized by heterogeneity in different regions of the cytoplasm of both algae, as well as by species specificity. The formation of the heteropolymeric MDH isozyme is restricted to a definite region of the cytoplasm of heterokaryons and nuclear-cytoplasmic A.crenulata-A.mediteranea hybrids at different stages of their development. The data obtained suggest that the concentrations of the free subunits of MDH, coded for by homologous genes, are unevenly distributed in the cytoplasm of hybrid cells. The heteropolymeric MDH isozyme in these cells is presumably the result of the de novo synthesis of isozyme subunits. This seems plausible inasmuch as no exchange occurs between the homopolymeric MDH isozymes of both parental types in the cytoplasm. The formation of the heteropolymeric MDH isozyme is tentatively related to the spatial compartmentalization of the mRNAs of homologous genes coding for the MDH subunits.

Analysis of mechanisms regulating the expression of parental alleles at the GPD locus in mule erythrocytes.

Erythrocyte glucose-6-phosphate dehydrogenase (G6PD) was examined by 13% starch gel electrophoresis in 74 mules (42 females and 32 males), 35 donkeys, and ten horses. The quantitative expression of the parental alleles at the Gpd locus varies greatly in female mules from the hemizygous expression of the maternal allele to that of the paternal. The data obtained indicate that the X chromosomes are randomly inactivated in females mules. No selective advantage of a cell population with a maternally (or paternally) derived X active was found in female mule erythrocytes. It is suggested that the phenotypic variability in the expression of the parental Gpd alleles is related to the random proportions established between cells having either a maternal or paternal X active in an initiator (stem) cell group giving rise to erythroid tissue. Initiator cell numbers estimated for erythroid tissue (six or seven) are close to those reported for human females and intergeneric fox hybrids. These numbers may vary depending on the duration of the time of determination and the division rate of initiator cells at determination.

Allelic expression in intergeneric fox hybrids (Alopex lagopus x Vulpes vulpes). II. Erythrocyte glucose-6-phosphate dehydrogenase in Artic and silver foxes: purification and properties.

The functional properties of purified glucose-6-phosphate dehydrogenase (G6PD) from the erythrocytes of Artic foxes (Alopex lagopus) and silver foxes (Vulpes vulpes) were investigated. It was found that pH optima for G6P D range from 8.15 to 8.25 in Arctic foxes and from 10.2 to 10.4 in silver foxes. For G6P, the estimated Km values were 74 X 10(-6) M (at pH 8.2) and 166 X 10(-6) M (at pH 10.2) in Artic foxes and 58 X 10(-6) M (at pH 10.2) and 40 X 10(-6) M (at pH 8.2) in silver foxes. The Km values for NADP were estimated as 62 X 10(-6) M (at pH 8.2) and 86 X 10(-6) M (at pH 10.2) in the Artic foxes and 15 X 10(-6) M (at pH 10.2) and 12 X 10(-6) M (at pH 8.2) in the silver foxes. It was found that Mg2+ ions exert a significant activating effect on G6P D in the Arctic fox and do not affect appreciably its activity in the silver fox. The experimental data indicate that slight differences in the electrophoretic mobility of G6P D are associated with considerable functional differences in this enzyme between the two fox species.

Allelic expression in intergeneric fox hybrids (Alopex lagopus x Vulpes vulpes). I. Comparative electrophoretic studies on blood enzymes and proteins in arctic and silver foxes.

Twenty-seven blood enzymes and proteins, whose structures are presumably controlled by at least 33 genes, were assayed in Arctic and silver foxes by starch gel electrophoresis. Two types of protein and enzyme electrophoretic patterns were distinguished: one exhibiting a single enzyme, the other several isozymes. The two fox species were found to differ in seven of the 27 enzymes and proteins studied: glucose-6-phosphate dehydrogenase, adenylate kinase, erythrocyte carboxylesterase, diaphorase, prealbumin, transferrin, and albumin. No differences were established between the species for the other enzymes and proteins. The data are interpreted as evidence for the existance of a set of enzymes and proteins differentiating the Arctic from the silver fox.