作者: J. Dissing , A.H. Johnsen , G.F. Sensabaugh
DOI: 10.1016/S0021-9258(18)54754-2
关键词: Phosphatase 、 Alanine 、 Enzyme 、 Biology 、 Isozyme 、 Biochemistry 、 Alternative splicing 、 Peptide sequence 、 Homology (biology) 、 Molecular biology 、 Acid phosphatase
摘要: The pair of isozymes, Bf and Bs, encoded by the human red cell acid phosphatase ACP1*B allele has been sequenced. Similar but not identical primary structures were observed. Both isozymes consist a single peptide chain 157 amino residues, which is acetylated at amino-terminal alanine residue. Bs are glycosylated, calculated molecular masses 17,932 17,867 Da, respectively. They except for sequence segment 40-73, peculiar to respective isozyme. This consistent with our hypothesis that two generated as result alternative splicing RNA transcript. finding signature offers basis characteristic differences in catalytic properties isozymes. A high degree homology was found between isozyme 18-kDa cytosolic from bovine liver. No observed other sequenced proteins, this establishes these low weight phosphatases products distinct gene family.