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Codfish muscle aldolase: Purification, properties, and primary structure around the substrate-binding site

Authors :
C.Y. Lai
C. Chen
Source :
Archives of Biochemistry and Biophysics. 144:467-475
Publication Year :
1971
Publisher :
Elsevier BV, 1971.

Abstract

FDP aldolase has been purified and crystallized from the muscle of codfish. The specific activity of the codfish enzyme was found to be two-thirds that of rabbit muscle aldolase. Other catalytic properties, the molecular weight, and the carboxyl-terminal structure were similar to those of rabbit muscle aldolase. A tryptic peptide containing the Schiff base-forming lysine (1) has been isolated and its primary structure determined as: Ala-Leu-Ser-Asp-His-His-Val-Tyr-Leu-Gln-Gly-Thr-Leu-Leu-βGlys-Pro-Asn-Met-Val-Thr-Ala-Gly-His-Ser-CMCys-Ser-His-Lys. Extensive homology observed in this region of the aldolase molecules isolated from biologically divergent sources indicates the importance of this structure for catalysis of the aldolase reaction.

Details

ISSN :
00039861
Volume :
144
Database :
OpenAIRE
Journal :
Archives of Biochemistry and Biophysics
Accession number :
edsair.doi.dedup.....15a265d40bef312bdfbea43ee8a12084