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Pep A5–1 and Pep A6–1: two new variants of peptidase A with features of special interest
Author(s) -
LEWIS W. H. P.,
CORNEY G.,
HARRIS HARRY
Publication year - 1968
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1968.tb00047.x
Subject(s) - allele , cysteine , biology , heterozygote advantage , residue (chemistry) , microbiology and biotechnology , genotype , genetics , lysine , population , biochemistry , amino acid , chemistry , enzyme , gene , medicine , environmental health
Summary 1. Two rare peptidase A phenotypes, Pep A 5–1 and Pep A 6–1, have been found in the course of population surveys of red cell peptidases. 2. Family studies indicate that they occur in heterozygotes. The two rare alleles have been designated Pep A 5 and Pep A 6 . The genotype of Pep A 5–1 may be written Pep A 1 Pep A 5 and that of Pep A 6–1 individuals Pep A 1 Pep A 6 . 3. The Pep A 5–1 electrophoretic pattern changes in a characteristic manner on storage of the haemolysate. It is suggested that the changes are due to reaction with oxidized glutathione which accumulates in haemolysates on storage. 4. Arguments are presented which suggest that the Pep A 6 allele codes for a variant poly‐peptide chain in which a cysteine residue has been substituted for a particular arginine residue in the polypeptide chain coded for by the common allele Pep A 1 . Also that the Pep A 6 allele codes for a variant polypeptide chain in which a glutamic acid residue is substituted for a particular lysine residue.