Actin from Heart Muscle: Sulfhydryl Groups

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Actin from Heart Muscle: Sulfhydryl Groups.

• A comparison of a number of chemical features of actin prepared from cardiac and skeletal muscle has been undertaken in an attempt to evaluate the role that this contractile protein may play in determining specific physiological responses by the two types of muscle. Analyses of physicochemical properties 1 and amino acid compositions failed to reveal significant differences between these prot...

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Sulfhydryl Groups in Proteins

Egg albumin in the native, unaltered state, does not give tests characteristic of sulfhydryl groups. When, however, this protein is treated in any one of several ways, such as by heat (8, 9, 17), ultraviolet irradiation (lo), shaking (lo), or by solution in urea or other amides (7), free sulfhydryl groups make their appearance. The amount of free -SH groups appearing in egg albumin through the ...

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Actin from Heart Muscle: Studies on Amino Acid Composition.

• The differences that exist between the physiological behavior of cardiac and skeletal muscle may be due, at least in part, to differences in their contractile proteins. For example, the relative weakness of cardiac muscle' 2 may be a reflection of a lesser contractile force developed by cardiac actomyosin.4 In view of these, and other observations, studies directed toward the detection of che...

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Actin from Heart Muscle: Isolation, Purification, and Physicochemical Properties.

• A comparison of the properties of cardiac actin with those of skeletal actin has been undertaken in an attempt to explain several fundamental differences between the behavior of heart and skeletal muscle which have recently been elucidated. Most striking among these is the finding that cardiac muscle develops less tension than its skeletal counterpart. Burton has calculated that the force gen...

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Sulfhydryl Groups and the Structure of Hemoglobin

1. Addition of 2 moles of mersalyl, mercuric chloride, p-chloromercuribenzoate (PCMB), or methyl mercury hydroxide per mole of hemoglobin greatly reduces heme-heme interactions (n), yet these substances have quite different effects on the oxygen affinity (-log p(50)). Mersalyl and mercuric chloride at this concentration each increase the oxygen affinity, while PCMB and methyl mercury have littl...

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ژورنال

عنوان ژورنال: Circulation Research

سال: 1964

ISSN: 0009-7330,1524-4571

DOI: 10.1161/01.res.14.4.345