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The primary sequence of the PFK‐1 inactivating zinc‐binding protein as deduced from cDNA sequencing Identity of the zinc‐binding protein with rat parathymosin
Author(s) -
Trompeter Hans-Ingo,
Brand Ingeborg A.,
Söling Hans-Dieter
Publication year - 1989
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 - 10.1016/0014-5793(89)80930-5
Subject(s) - zinc , zinc finger , complementary dna , sequence (biology) , biology , binding protein , protein sequencing , genetics , biochemistry , peptide sequence , microbiology and biotechnology , chemistry , gene , transcription factor , organic chemistry
We have recently described the sequence of the Zn 2+ ‐binding domain (43 amino acid residues) of a newly detected Zn 2+ ‐binding protein which reversibly inactivates phosphofructokinase‐1 in a Zn 2+ ‐dependent manner [(1986) J. Biol. Chem. 269, 5895–5900; (1988) Eur. J. Biochem. 177, 561–568]. Here, we describe the primary sequence of this protein based on a full‐length cDNA. A sequence comparison reveals the identity of the Zn 2+ ‐binding protein with a protein called parathymosin‐α.