Some properties of trypsin-like proteases extracted from the seaweed Codium fragile and their purification

Two enzymes were purified from the green alga Codium fragile , collected in 1988 at Fukuoka, Japan, by batch-wise ion-exchange extraction, affinity chromatography and ion-exchange high-performance liquid chromatography (HPLC) using Boc-Ala-Ala-Pro-Arg-pNA as a substrate. The molecular weights of the...

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Bibliographic Details
Published in:Marine biology 1990-01, Vol.107 (3), p.513-517
Main Authors: KADOKAMI, K, YOSHIDA, N, MIZUSAKI, K, NODA, K, MAKISUMI, S
Format: Article
Language:English
Subjects:
Biological and medical sciences
Cell biochemistry
Cell physiology
Codium fragile
Fundamental and applied biological sciences. Psychology
Marine
Plant physiology and development
trypsin
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Summary:Two enzymes were purified from the green alga Codium fragile , collected in 1988 at Fukuoka, Japan, by batch-wise ion-exchange extraction, affinity chromatography and ion-exchange high-performance liquid chromatography (HPLC) using Boc-Ala-Ala-Pro-Arg-pNA as a substrate. The molecular weights of the enzymes were estimated as 38,000 and 39,000, using gel filtration HPLC. The enzymes had the same optimal pH range of 7 to 9 for both activities, and an exclusively hydrolyzed peptide bond on the carboxyl-terminal side of the L-arginine of peptide p-nitroanilides. The ratios of the enzymatic activity for X-Arg-pNA to X-Lys-pNA were larger than 100. The enzymes exhibited 30 times higher activity toward Boc-Ala-Ala-Pro-Arg-pNA when compared with trypsin.
ISSN:0025-3162
1432-1793
DOI:10.1007/BF01313436