The heat of hydrolysis of thiolacetic acid

1957 ◽  
Vol 53 (0) ◽  
pp. 455-459 ◽  
Author(s):  
S. Sunner ◽  
I. Wadsö
Keyword(s):  
Hydrolysis Of ◽  
Thiolacetic Acid ◽  
Heat Of Hydrolysis

The heat of hydrolysis of boron tribromide

1955 ◽  
Vol 51 ◽  
pp. 19 ◽  
Author(s):  
H. A. Skinner ◽  
N. B. Smith
Keyword(s):  
Boron Tribromide ◽  
Hydrolysis Of ◽  
Heat Of Hydrolysis

scholarly journals The Heat of Hydrolysis of i-Propenyl Acetate and m-Cresyl Acetate and the Heat of Enolization of Acetone.

1957 ◽  
Vol 11 ◽  
pp. 1757-1760 ◽  
Author(s):  
S. Sunner ◽  
Johan J. Lothe ◽  
K. Lunde ◽  
J. Schliack ◽  
L. Reio
Keyword(s):  
Hydrolysis Of ◽  
Heat Of Hydrolysis

Heat of hydrolysis of trimetaphosphate

1953 ◽  
Vol 12 (1-2) ◽  
pp. 121-127 ◽  
Author(s):  
Otto Meyerhof ◽  
Romas Shatas ◽  
Ann Kaplan
Keyword(s):  
Hydrolysis Of ◽  
Heat Of Hydrolysis

scholarly journals Enzymatic Activity in the M Band

1959 ◽  
Vol 6 (2) ◽  
pp. 163-170 ◽  
Author(s):  
Russell J. Barrnett ◽  
George E. Palade
Keyword(s):  
Electron Microscopy ◽  
Enzymatic Hydrolysis ◽  
Enzymatic Activity ◽  
Striated Muscles ◽  
Histochemical Reaction ◽  
Esterase Inhibitors ◽  
Enzymatic Nature ◽  
Hydrolysis Of ◽  
Thiolacetic Acid

Experiments which combined histochemistry and electron microscopy were performed in studying the sites of enzymatic hydrolysis of thiolacetic acid in the presence of lead ions in diaphragmatic and cardiac muscle. It was found that in these striated muscles the electron opaque, final product of the histochemical reaction (PbS) was discretely deposited on the swelling of the thick elemental filaments that occurs at the M band. Additional sites of enzymatic activity occurred in mitrochondria and in round sarcoplasmic bodies. A reaction, probably non-enzymatic, also occurred in contraction bands in the area of the Z bands and in the sarcoplasmic reticulum. To ascertain the enzymatic nature of the reaction and to define the enzyme involved, control experiments were carried out and the effect of various esterase inhibitors was assayed. It is suggested that the M band enzyme is a cholinesterase, but the enzymes in the mitochondria and the sarcoplasmic bodies that hydrolyze the substrate appear to be different. A possible role of the M band enzyme is discussed.

The Effect of Ionic Strength on the Heat of Hydrolysis of Benzoyl-L-argininamide1

1956 ◽  
Vol 78 (7) ◽  
pp. 1349-1352 ◽  
Author(s):  
Waldie W. Forrest ◽  
Herbert Gutfreund ◽  
Julian M. Sturtevant
Keyword(s):  
Ionic Strength ◽  
Hydrolysis Of ◽  
Heat Of Hydrolysis

scholarly journals THE USE OF THIOL-SUBSTITUTED CARBOXYLIC ACIDS AS HISTOCHEMICAL SUBSTRATES

1965 ◽  
Vol 13 (8) ◽  
pp. 611-628 ◽  
Author(s):  
MARY BELL ◽  
RUSSELL J. BARRNETT
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Lipid Metabolism ◽  
Light Microscopy ◽  
Nuclear Envelope ◽  
Carboxylic Acids ◽  
Structural Level ◽  
Low Concentrations ◽  
Hydrolysis Of ◽  
Thiolacetic Acid

Thiobutyric, thiocaproic and thiocaprylic acids were synthesized, and enzyme histochemical methods were developed using these thiol-substituted carboxylic acids, as well as thiolacetic acid, as substrates with Pb++ as the capture reagent. The localization of final product of these histochemical reactions, PbS, was studied and compared in a variety of tissues with light microscopy. The enzymatic activities demonstrated were sensitive to low concentrations of E600. The localization of these reactions in several intensely reactive tissues, liver, testis and intestine, were also studied with electron microscopy. At a fine structural level, the final product was deposited primarily in relation to the membranous elements of the smooth and rough varieties of the endoplasmic reticulum, including the nuclear envelope, and of mitochondria. The results of these experiments are discussed, including the possible identity of the enzymes concerned with the hydrolysis of the thiol-substituted substrates. It was suggested that at least three activities were demonstrated in these experiments, one of which was the B type esterase of microsomes, and all of which functioned in lipid metabolism.

Heat of hydrolysis of some phosphate compounds

1952 ◽  
Vol 36 (2) ◽  
pp. 411-420 ◽  
Author(s):  
Paul Ohlmeyer ◽  
Romas Shatas
Keyword(s):  
Hydrolysis Of ◽  
Heat Of Hydrolysis ◽  
Phosphate Compounds
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