Peptidoglycan hydrolytic activities associated with bacteriophage virions
نویسندگان
چکیده
منابع مشابه
Protein kinase activities associated with the virions of pseudorabies and herpes simplex virus.
Protein kinase has been extracted in soluble form from virions of pseudorabies virus using 10% NP40, 0.6 M-NaCl. Chromatographic analysis of the extract on DEAE-cellulose and on phosphocellulose showed it to contain more than one kinase. The activity responsible for the phosphorylation of the major phosphoproteins (mol. wts. 120 000, 115 000 and 72 000) of virions was found to be similar in its...
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A protein kinase activity has been found associated with purified Sendai virions. Most of the virion proteins and exogenous protamine served as substrates for this enzyme.
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Histochemical observations were carried out on various hydrolytic enzymes in the spontaneous mammary carcinoma of C3H-strain mice. Alkaline phosphatase activity was observed in the luminal border of the tubular structure and in the periluminal surface, which showed a cystic dilatation in ducts and papillae. Capillaries in the stroma showed a high enzymatic activity. Acid phosphatase activity wa...
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Peptidoglycan (PG) is an essential component in the cell wall of nearly all bacteria, forming a continuous, mesh-like structure, called the sacculus, around the cytoplasmic membrane to protect the cell from bursting by its turgor. Although PG synthases, the penicillin-binding proteins (PBPs), have been studied for 70 years, useful in vitro assays for measuring their activities were established ...
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A group B streptococcal (GBS) bacteriophage lysin gene was cloned and expressed in Escherichia coli. The purified recombinant enzyme, calculated to have a molecular mass of 49 677 Da, lysed GBS cells. The susceptibility of GBS cells to lysis by the enzyme depended upon the growth stage at which they were harvested, with early exponential phase cells most sensitive. Calcium ions enhanced the act...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2003
ISSN: 0950-382X
DOI: 10.1046/j.1365-2958.2003.03894.x