SPECIFICITY OF A MILK CLOTTING ENZYME EXTRACTED FROM THE THISTLE CYNARA-CARDUNCULUS L - ACTION ON OXIDIZED INSULIN AND K-CASEIN

K-casein and oxidised insulin were digested with an acid protease extracted from Cynara cardunculus L. The fragments produced were isolated and characterised. In k-casein cleavage occured specifically at Phe105-Met106 bond. In oxidised insulin seven fragments were obtained and cleavage was found to...

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Bibliographic Details
Published in:Biotechnology letters 1992-09, Vol.14 (9), p.841-846
Main Authors: FARO, CJ, MOIR, AJG, PIRES, EV
Format: Article
Language:English
Subjects:
amino acids
Biological and medical sciences
Biotechnology
Biotechnology & Applied Microbiology
casein
Cynara cardunculus
Enzyme engineering
Fundamental and applied biological sciences. Psychology
insulin
Life Sciences & Biomedicine
Methods. Procedures. Technologies
milk-clotting enzymes
Miscellaneous
proteinase
Science & Technology
specificity
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Summary:K-casein and oxidised insulin were digested with an acid protease extracted from Cynara cardunculus L. The fragments produced were isolated and characterised. In k-casein cleavage occured specifically at Phe105-Met106 bond. In oxidised insulin seven fragments were obtained and cleavage was found to occur at the carboxylic side of (Phe, Leu, Ile)-X, where X was preferentially Val or Tyr. The results obtained with insulin B chain suggest that Cynara cardunculus L. protease possesses a greater specificity than other acid proteases reported.
ISSN:0141-5492
1573-6776
DOI:10.1007/BF01029150