scholarly journals Enzymatic Activity in the M Band

1959 ◽  
Vol 6 (2) ◽  
pp. 163-170 ◽  
Author(s):  
Russell J. Barrnett ◽  
George E. Palade

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.

2016 ◽  
Vol 199 ◽  
pp. 49-58 ◽  
Author(s):  
Shaoni Sun ◽  
Shaolong Sun ◽  
Xuefei Cao ◽  
Runcang Sun

1993 ◽  
Vol 97 (43) ◽  
pp. 11344-11349 ◽  
Author(s):  
Adam W. Mazur ◽  
Janet L. Burns ◽  
George D. Hiler ◽  
Richard J. Spontak

BioResources ◽  
2019 ◽  
Vol 14 (1) ◽  
pp. 1653-1667
Author(s):  
Yawen Zhou ◽  
Jian Yang ◽  
Cong Luo ◽  
Bo Yang ◽  
Changyao Liu ◽  
...  

The effect of metal ions and surfactants on the enzymatic hydrolysis of pretreated wheat straw lignocellulose was investigated. Scanning electron microscopy, infrared spectrum analysis, dynamic light scattering, and fluorescence spectra analysis were used to characterize the influence of Fe3+/ polyoxyethylene (20) sorbitan monooleate (Tween 80). The interaction between Fe3+/Tween 80 and enzyme was further investigated by enzyme kinetics and enzyme activity measurements. The best synergistic effect was obtained when the ratio of Fe3+ and Tween 80 was 0.06. The scanning electron microscopy images showed that the Fe3+/Tween 80 combination was associated with high porosity substrates. The infrared spectrum analysis indicated that the components of the substrates depended on additive types. The highest relative enzymatic activity increase rate was obtained with added Fe3+/ Tween 80. The Vmax and Km values of the group with added Fe3+/Tween 80 were much higher than that of the group without additives. With the addition of Fe3+/ Tween 80, the intensity of the fluorescence emission peak decreased and the peak shifted towards a longer wavelength.


1965 ◽  
Vol 13 (8) ◽  
pp. 611-628 ◽  
Author(s):  
MARY BELL ◽  
RUSSELL J. BARRNETT

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.


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