Effect of ATP on release of intracellular enzymes from damaged cells

Nature ◽  
1974 ◽  
Vol 249 (5458) ◽  
pp. 662-663 ◽  
Author(s):  
J. H. WILKINSON ◽  
JEAN M. ROBINSON
Keyword(s):  
Intracellular Enzymes

Intracellular enzymes of collagen biosynthesis in rat kidney in streptozotocin diabetes

Diabetes ◽  
1976 ◽  
Vol 25 (11) ◽  
pp. 1066-1070 ◽  
Author(s):  
J. Risteli ◽  
V. A. Koivisto ◽  
H. K. Akerblom ◽  
K. I. Kivirikko
Keyword(s):  
Rat Kidney ◽  
Streptozotocin Diabetes ◽  
Collagen Biosynthesis ◽  
Intracellular Enzymes

scholarly journals Intracellular serine proteinase of Bacillus subtilis strain Marburg 168. Comparison with the homologous enzyme from Bacillus subtilis strain A-50

1979 ◽  
Vol 179 (2) ◽  
pp. 333-339 ◽  
Author(s):  
A Y Strongin ◽  
D I Gorodetsky ◽  
I A Kuznetsova ◽  
V V Yanonis ◽  
Z T Abramov ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Serine Proteinase ◽  
Subtilis Strain ◽  
Bacterial Strains ◽  
Terminal Sequence ◽  
Gramicidin S ◽  
Intracellular Enzymes ◽  
Sepharose 4B ◽  
Homologous Enzyme ◽  
Strict Selection

Intracellular serine proteinase was isolated from sporulating cells of Bacillus subtilis Marburg 168 by gramicidin S-Sepharose 4B affinity chromatography. The enzymological characteristics, the amino acid composition and the 19 residues of the N-terminal sequence of the enzyme are reported. The isolated proteinase was closely related to, but not completely identical with, the intracellular serine proteinase of B. subtilis A-50. The divergence between these two intracellular enzymes was less than that between the corresponding extracellular serine proteinases (subtilisins) of types Carlsberg and BPN′!, produced by these bacterial strains. This may be connected with the more strict selection constraints imposed in intracellular enzymes during evolution.

Controlled lysis of bacterial cells utilizing mutants with defective synthesis of D-alanine

1988 ◽  
Vol 34 (3) ◽  
pp. 256-261 ◽  
Author(s):  
Michael P. Heaton ◽  
Robert B. Johnston ◽  
Thomas L. Thompson
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Cell Walls ◽  
Alanine Racemase ◽  
Growth Media ◽  
Bacterial Cells ◽  
Cell Wall Formation ◽  
Fermentation Processes ◽  
Intracellular Enzymes ◽  
Dense Cell

An alanine racemase (EC 5.1.1.1) mutant (Dal−) of Bacillus subtilis required small amounts of D-alanine to synthesize an osmotically stable cell wall in certain growth media. Investigation of the conditions which caused lysis in hypotonic media revealed that in addition to complex media, such as nutrient broth and acid-hydrolyzed casein, glycine inhibited stable cell wall formation. D-Alanine prevented the glycine inhibition. Up to 99% lysis occurred in both dilute and dense cell suspensions (optical densities up to 110) within 2.5 h after adding 1% glycine to late log phase cultures. Intracellular enzymes recovered from the lysate were as active as those from lysozyme-disrupted cells. No amino acid tested other than glycine induced lysis. Dal− mutants can be used for controlled lysis of bacterial cells to facilitate the isolation of normal intracellular constituents and bioengineered products from fermentation processes. Cell walls of most bacteria contain D-alanine; thus, this strategy should be applicable to a wide variety of microorganisms.

Detergent permeabilized yeast cells as the source of intracellular enzymes for estimation of biomolecules

1993 ◽  
Vol 15 (9) ◽  
pp. 796-800 ◽  
Author(s):  
Nayantara Bhat ◽  
N.S. Naina ◽  
L.R. Gowda ◽  
S.G. Bhat
Keyword(s):  
Yeast Cells ◽  
Intracellular Enzymes

Calcium-Dependent Proteases: A Prevalent Proteolytic System of Uncertain Function

Physiology ◽  
1987 ◽  
Vol 2 (3) ◽  
pp. 82-85
Author(s):  
GN DeMartino ◽  
DE Croall
Keyword(s):  
Animal Species ◽  
Regulatory Proteins ◽  
Proteolytic System ◽  
Calcium Dependence ◽  
Calcium Dependent ◽  
Intracellular Processing ◽  
Intracellular Enzymes ◽  
Micromolar Range

Calcium-dependent proteases are found in a wide variety of tissues from many animal species. They are intracellular enzymes that for activation require calcium in the micromolar range. In addition to the calcium dependence, two regulatory proteins have been identified, one an inhibitor and one an activator. These interactions indicate a highly complex role for calcium-dependent proteolysis in the intracellular processing of proteins.

Ultrasonic Effects on lsoenzymes

1966 ◽  
Vol 12 (4) ◽  
pp. 181-186 ◽  
Author(s):  
Clyde A Dubbs
Keyword(s):  
Human Serum ◽  
Ultrasonic Treatment ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Serum Cholinesterase ◽  
Starch Gel Electrophoresis ◽  
Selective Activation ◽  
Intracellular Enzymes ◽  
Starch Gel

Abstract Several significant effects of ultrasonic treatment on human serum cholinesterase and aminopeptidase isoenzymes and on other serum proteins have been found by starch gel electrophoresis. The selective activation of one cholinesterase isoenzyme is especially striking. These effects must be considered when ultrasonic treatment is used for the extraction of intracellular enzymes. When the effects are appreciated, ultrasonics should provide a valuable tool for isoenzyme research.

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