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Molecular heterogeneity of the cDNA encoding a 74‐kDa regulatory subunit (B″ or δ) of human protein phosphatase 2A 1
Author(s) -
Tanabe Osamu,
Gomez Gloria A,
Nishito Yasumasa,
Usui Hirofumi,
Takeda Masao
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00392-x
Subject(s) - gene isoform , protein subunit , complementary dna , isozyme , biology , microbiology and biotechnology , alternative splicing , cdna library , amino acid , biochemistry , phosphatase , peptide sequence , antiserum , residue (chemistry) , gene , enzyme , genetics , antibody
Two cDNAs for possible splicing variants of a 74‐kDa regulatory subunit (B″ or δ) of human protein phosphatase 2A, were isolated. These variants were identified from human cerebral cortex by library screening and PCR, and designated δ1 and δ3 isoforms, while the previously reported isoform [Tanabe et al. (1996) FEBS Lett. 379, 107–111] was designated δ2. Compared with the δ2 isoform, the δ1 isoform contained a 32‐residue insertion beginning at residue 84, and consisted of 602 amino acids in all. The δ3 isoform lacked a 74‐residue sequence corresponding to residues 1083 of the δ2 isoform, and consisted of 496 amino acids. Using isoform‐specific antipeptide antisera, the 74‐kDa subunit (B″ or δ) originally purified from human erythrocytes was identified as the δ1 isoform.