Robert J. Tanis

Additional data on the population distribution of human serum albumin genes; three new variants

Each albumin variant, its source, and ethnic origin are listed in the Appendix. Many of the new variants were found in several individuals in a single family. In other cases the variants were found in one or more individuals in a single village. The electrophoretic comparisons were made in the three starch-gel systems, acetate-EDTA at pH 5.0, tris-lithium-succinate-citrate at pH 6.0 and tris-EDTA-borate at pH 6.9, used previously (Weitkamp et al. 1973). RESULTS The results of the comparison of 30 new or recently described serum albumin variants with 20 variants previously distinguished using three starch-gel electrophoretic systems are presented in Table 1. Although the amount of separation reported here for the 20 variants previously described differs slightly from the earlier results, due to minor variations in electrophoretic conditions, the conclusions regarding their mobility relative to normal albumin and to each other remain the same. Three new variants, RS I, Xavante, and Yanomama-2, all slowly migrating, have been identified. Electropherograms showing these variants adjacent

Genetic studies of the Macushi and Wapishana Indians

SummaryBlood samples from 509 Macushi and 623 Wapishana Amerindians of Northern Brazil and Southern Guyana have been analyzed with reference to the occurrence of rare variants and genetic polymorphisms of the following 25 systems: (i) Erythrocyte enzymes: acid phosphatase-1, adenosine deaminase, adenylate kinase-k, carbonic anhydrase-1, carbonic anhydrase-2, esterase A1,2,3, esterase D, galactose-1-phosphate uridyltransferase, isocitrate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, nucleoside phosphorylase, peptidase A, peptidase B, phosphoglucomutase 1, phosphoglucomutase 2, phosphogluconate dehydrogenase, phosphohexoseisomerase, triosephosphate isomerase and (ii) Serum proteins: albumin, ceruloplasmin, haptoglobin, hemoglobin A, hemoglobin A2 and transferrin. Fifteen different rare variants were detected, involving 11 of these systems. In addition, a previously undescribed variant of ESA1,2,3 which achieves polymorphic proportions in both these tribes is described. Excluding this variant, the frequency of rare variants is 1.1/1000 in 12510 determinations in the Macushi and 4.7/1000 in 15 396 determinations in the Wapishana. The ESA1,2,3, polymorphism was not observed in 382 Makiritare, 232 Yanomama, 146 Piaroa, 404 Cayapo, 190 Kraho and 112 Moro. Irregularities in the intratribal distribution of this polymorphism in the Macushi and Wapishana render a decision as to the tribe of origin impossible at present. Gene frequencies are also given for previosly described polymorphisms of 5 systems: haptoglobin, phosphoglucomutase 1, erythrocyte acid phosphatase, esterase D, and galactose-1-phosphate-uridyl-transferase.

The frequency in Japanese of genetic variants of 22 proteins. I. Albumin, ceruloplasmin, haptoglobin, and transferrin.

This paper presents the results of an electrophoretic survey of approximately 4000 individuals from the cities of Hiroshima and Nagasaki, Japan, for four serum proteins: albumin, ceruloplasmin, haptoglobin and transferrin. The haptoglobin gene frequencies obtained for the HP1‐HP2 polymorphism are in agreement with earlier reports. Rare electrophoretic variants of albumin, ceruloplasmin and haptoglobin occur with frequencies of 2.48, 0.50 and 0.58 per 1000 determinations, respectively. The noteworthy finding of 8 distinct transferrin variants in these populations, with a combined frequency of 20.90 per 1000 determinations, is also presented. Four of these variants (DCh1, B1, B3 and Dhir2 which corresponds electrophoretically to D4) have been reported in other populations in Japan, but the other five have not previously been differentiated.

Amino acid sequence of sheep carbonic anhydrase C

Abstract The sequence of amino acid residues comprising the major form of sheep red cell carbonic anhydrase C has been determined. The primary sequences of peptides derived from cyanogen bromide cleavage and tryptic digestion were obtained primarily through the use of the Edman degradation procedure. The ordering of these peptides in the sheep molecule is based on the high degree of homology between the sheep enzyme and the previously sequenced human and bovine carbonic anhydrase C molecules. Based on comparisons with the three-dimensional structure of human carbonic anhydrase C, the function of certain residues which appear to be involved either in the maintenance of structure or in the active site of the sheep enzyme is discussed.

Amino acid sequence of rabbit carbonic anhydrase II.

The amino acid sequence of the high activity form of erythrocyte carbonic anhydrase, carbonic anhydrase II, purified from rabbit erythrocytes has been determined. This sequence was determined primarily from the cyanogen bromide and tryptic peptides through use of automated Edman degradation procedures. The ordering of the peptides from rabbit carbonic anhydrase II was based on the high degree of homology between the rabbit enzyme and the homologous enzymes derived from sheep, bovine, and human erythrocytes. The function of certain residues is discussed in the context of these three known sequences and the previously reported three-dimensional structure of human carbonic anhydrase II. Possible microheterogeneity of rabbit carbonic anhydrase II is also discussed.

The frequency in Japanese of genetic variants of 22 proteins V. Summary and comparison with data on Caucasians from the British Isles

The frequencies in Hiroshima and Nagasaki of rare variants (represented in less than 2 % of the individuals surveyed) is summarized for a series of 22 proteins (25 polypeptides). The average number of persons examined for each protein was 3312. There are three pairs of homologous proteins in the series: PGM, and PGM, CA I and CA 11, and HGB A and A,. Only for the first pair is there a significant difference between the two in the total frequency and number of different kinds of variants; it is suggested this may reflect differences in the mutation rates of the corresponding structural genes. For 23 of these polypeptides, comparable data are available for British Caucasians. The average frequency of variants for loci in common in the two series is 2.0/1000 person determinations for Japanese and 1.6/1000 for Caucasoids. At two loci (PGMl and PHI) there were significantly more variants in Japanese than in British; these two loci account for the greater average frequency of variants in Japanese. However, a conservative comparison of number of diflerent variants (electromorphs) encountered, using the 0 statistic of Ewens (1972), yields no significant difference for any of the 22 possible contrasts. The potential usefulness of data of this type in reaching conclusions regarding comparability of mutation rates in two populations is discussed. For the present, the fact that one electromorph may shelter multiple different amino acid substitutions in a protein limits the inferences to be drawn from such contrasts.

Evolution of Carbonic Anhydrase in Primates and Other Mammals

The carbonic anhydrases are especially well suited for studies on molecular evolution for a variety of reasons: (1) In many mammals, two isozymes of carbonic anhydrase which appear to be products of two closely linked genes are present in the red cells. (2) They are able to incorporate mutational changes at relatively rapid rates. (3) They can be readily isolated in pure form from hemolysates. (4) They appear to be involved in a variety of important physiological functions where their specific catalytic role is the interconversion of CO2 and HCO 3 - . For reviews, see Lindskog et al. (1971) and Tashian and Carter (1976).

Amino acid sequence of the coat protein subunit in satellite tobacco necrosis virus

Abstract The primary structure of the coat protein subunit in satellite tobacco necrosis virus has been investigated. The results obtained are consistent with and support the proposal for the amino acid sequence made from the nucleotide sequence of RNA (Ysebaert et al., 1980). This would imply that no intervening sequences of RNA occur in the cistron for the satellite tobacco necrosis virus coat protein. The polypeptide chain of the protein consists of 195 amino acid residues. It contains one sulfhydryl group but no disulfide bridges. The distribution of various kinds of amino acid residues along the chain is markedly uneven.

The amino acid sequence of carbonic anhydrase I from the rhesus macaque.

Abstract The complete amino acid sequence of carbonic anhydrase I (CA I) isolated from the red cells of the rhesus macaque ( Macaca mulatta ) is presented. This sequence was obtained by aligning peptides derived from various fragmentation procedures with the fully characterized sequence of human CA I. When the peptides of rhesus CA I were ordered in this manner, 13 of the 260 residues were found to differ from the human CA I sequence. The known markedly higher specific esterase activity of rhesus CA I compared to human CA I could not be correlated with any changes in residues postulated to be within 10 A of the single zinc ion at the active site.

Differential rates of evolution in the carbonic anhydrase isozymes of catarrhine primates

Abstract Homologous regions of the primary sequences of the two red cell carbonic anhydrase isozymes, CA I and CA II, were compared in Man, two great apes, three catarrhine monkeys, and sheep for 115 shared codon positions. These sequences comprised approximately 45% of the complete sequences of the isozyme molecules that were compared. A maximum parsimony method was used to determine the minimum number of nucleotide changes in the different lines of descent. An apparent slowing down in the rate of incorporation of mutational changes was indicated for both isozymes in the primate species examined. This deceleration was considerably more marked in the high-activity isozyme, CA II, than in the low-activity form, CA I.