HUMAN RED-CELL ACID-PHOSPHATASE (ACP1) - THE PRIMARY STRUCTURE OF THE 2 PAIRS OF ISOZYMES ENCODED BY THE ACP1-ASTERISK-A AND ACP1-ASTERISK-C ALLELES

被引:28
作者
DISSING, J [1 ]
JOHNSEN, AH [1 ]
机构
[1] UNIV COPENHAGEN,RIGSHOSP,DEPT CLIN BIOCHEM,DK-2100 COPENHAGEN,DENMARK
关键词
AMINO ACID SEQUENCE; ALTERNATIVE SPLICING; ALLELIC PRODUCT; CYTOSOLIC; SIGNATURE SEQUENCE; ERYTHROCYTE;
D O I
10.1016/0167-4838(92)90155-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Af, As, Cf and Cs isozymes encoded by the human red cell acid phosphatase ACP1*A and ACP1*C alleles, respectively, have been sequenced. All four isozymes consist of a single non-glycosylated peptide chain (157 residues), acetylated at the amino-terminal alanine residue. Each f isozyme differs from the corresponding s isozyme over the sequence segment 40-73, while the remaining four-fifth of the molecules are identical. These findings are consistent with results for the Bf and Bs isozymes encoded by the common ACP1*B allele and confirm that the presence of a specific f or s segment is a common property to ACP1 isozymes. This supports our hypothesis that f and s isozymes are generated by alternative splicing of exons in the primary RNA transcript. Cf and Cs are identical in sequence with Bf and Bs, respectively. Thus, the ACP1*B and ACP1*C alleles encode exactly the same pair of isozymes, the only difference at the protein level being the ratio of f and s isozyme. Af and As differ from the Bf and Bs isozymes by a single substitution at residue 105; Arg and Gln, respectively. These observations explain the electrophoretic identity of the B and C isozyme pairs and the higher P(i) of the A isozyme pair.
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页码:261 / 268
页数:8
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