PROPERTIES OF PROTEINASE FROM STREPTOCOCCUS FAECALIS VAR. LIQUEFACIENS
نویسندگان
چکیده
منابع مشابه
Stimulation of proteinase biosynthesis by canavanine in streptococcus faecalis var. liquefaciens.
l-Canavanine, an analogue of arginine, was found to stimulate the synthesis of an extracellular proteinase in Streptococcus faecalis var. liquefaciens. Cells grown in a synthetic medium containing 10(-4)m arginine and 10(-4)m canavanine produced almost twice as much proteinase as cells grown in 2 x 10(-3)m arginine alone; total growth was the same in both media. Hydrolyzed proteinase samples we...
متن کاملGrowth of Streptococcus faecalis var. liquefaciens on plants.
The proliferation of Streptococcus faecalis var. liquefaciens on two varieties of beans, and on corn, rye, and cabbage was investigated. Comparisons were made with growth patterns on these same plants exhibited by S. lactis and Lactobacillus plantarum. The ability of each of the bacteria to multiply and to spread to new plant parts as they developed from seed was studied under several environme...
متن کاملGrowth Stimulation of Streptococcus Faecalis Var. Liquefaciens by Canavanine.
Hammel, Jay M. (The Pennsylvania State University, University Park) and L. N. Zimmerman. Growth stimulation of Streptococcus faecalis var. liquefaciens by canavanine. J. Bacteriol. 86:490-493. 1963.-l-Canavanine, a competitive inhibitor of arginine, was found to stimulate the growth of Streptococcus faecalis var. liquefaciens in the presence of arginine. This growth stimulation by canavanine wa...
متن کاملEffect of carbon dioxide on the aspartic acid requirement for proteinase biosynthesis by Streptococcus faecalis var. liquefaciens.
Non-proliferating cells of Streptococcus faecalis var. liquefaciens required aspartic acid for proteinase biosynthesis in the absence of CO(2) but not in the presence of CO(2).
متن کاملDependence of protease secretion by Streptococcus faecalis var. liquefaciens on arginine and its possible relation to site of synthesis.
Washed cells of Streptococcus faecalis var. liquefaciens, when harvested from media that supported protease biosynthesis, continued to release this extracellular enzyme in phosphate buffer. The addition of ethylenediaminetetraacetic acid (EDTA) halted the secretion. If zinc ions were added to the EDTA-treated cells before 45 to 60 min had elapsed, a fraction of the anticipated enzyme activity w...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1964
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.88.3.653-659.1964