Purification and Characterization of L-Arginine Deiminase from Vibrio Alginolyticus 1374
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چکیده
منابع مشابه
Purification and some properties of a novel L-2,4-diaminobutyric acid decarboxylase from Vibrio alginolyticus.
Previous investigations have shown that members of the genus Vibrio possess a novel enzyme activity decarboxylating L-2,4-diaminobutyric acid (DABA) to 1,3-diaminopropane (DAP). In this paper we describe the purification, by about 3600-fold, of the enzyme from V. alginolyticus. The purified enzyme was apparently homogeneous, and had a specific activity of 4200 nmol DAP min-1 (mg protein)-1. The...
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Arginine deiminase from the extreme halophilic archaebacterium Halobacterium salinarium was purified to homogeneity in a four-step procedure with a 310-fold enrichment. The enzyme consists of two identical subunits of 55 kDa; its native molecular mass is 105 kDa. The pI of 4.7 indicates that acidic nature of the protein, which is evidenced by its amino acid composition, which shows an excess of...
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Hydrodynamic, chemical, and optical properties of arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis are reported for the enzyme isolated from log phase cells. The s& +, and D’& values of the enzyme are 5.48 S and 5.87 x 10V7 cm’/s, respectively; the molecular weight is 87,300. Determination of the amino acid composition shows that about 45% of the residues are nonpolar. Another unique...
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Crystalline L-arginine deiminase of Pseudomonas putida was prepared by the following steps: sonic disruption, ammonium sulfate fractionation, protamine sulfate treatment, DEAE-cellulose column chromatography, and L-arginine-Sepharose 6B chromatography followed by crystallization. This procedure yields a crystalline pure enzyme with a 45% recovery of the activity in crude cell-free extracts. The...
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ژورنال
عنوان ژورنال: Journal of Pharmaceutical Research
سال: 2016
ISSN: 2454-8405,0973-7200
DOI: 10.18579/jpcrkc/2016/15/1/93748