Studies of Phospholipid-requiring Bacterial Enzymes
نویسندگان
چکیده
منابع مشابه
Studies on Bacterial Enzymes
The meningococcus cell contains a peptonase enzyme which hydrolyzes the peptides and similar constituents of commercial "peptone." The activity of this enzyme is independent of the presence of the formed bacterial cell. The peptonase enzyme is more resistant to heat and to oxidation than is the maltase enzyme of the same bacteria.
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Haemophilus parainfluenzae incorporates glycerol and phosphate into the membrane phospholipids without lag during logarithmic growth. In phosphatidyl glycerol (PG), the phosphate and unacylated glycerol moieties turn over and incorporate radioactivity much more rapidly than does the diacylated glycerol. At least half the radioactivity is lost from the phosphate and unacylated glycerol in about ...
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During the course of studies on the effect of vitamin K on several respiratory chain enzymes from 1VIycobacterium phlei, it was found that the soluble fraction contained a unique enzyme which required vitamin K suspended in phospholipid for the reduction of thiazolyl blue tetrazolium by malate. Malate oxidation in most tissues is catalyzed by the classical pyridine nucleotide-linked malic dehyd...
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Phosphatidyl ethanolamine and lipopolysaccharide were extracted and purified from the cell envelope fractions of Escherichia coli and Salmonella typhimurium. The two components were studied separately and after recombination, by use of electron microscopy and monolayer techniques, and by measuring their ability to participate in the enzyme-catalyzed uridine diphosphate-galactose:lipopolysacchar...
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Bacterial enzyme Hyaluronidase is a complex polysaccharide degrading enzyme that cleaves â-GlcNAc-(14) glycosidic linkage of Hyaluronate (HA) by â-elimination process. It is synthesized by a spectrum of grampositive bacteria which serve as potential contributors to a multitude of infectious diseases in human beings. Especially, group A streptococcus bacteria (GAS) have evolved several orders...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)45470-7