ISSN:
1573-4919
Keywords:
arginine aminopeptidase
;
enzyme activation
;
chelation
;
divalent cation
;
Streptococcus mitis
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Abstract Activation of Streptococcus mitis (ATTC 9811) arginine aminopeptidase resulted in removal of the metal(s) from the enzyme molecule, and the action of the heavy metal ion in the inactivation process was shown to involve formation of a chelate complex between the enzyme molecule and metal or oxidation of functional group(s) on the enzyme surface. The enzyme also underwent activation by bovine serum albumin, amino acids, phosphate, and citric acid, which are probable physiological chelators.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00219425
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