DISTRIBUTION OF PROTEIN-BOUND SULFHYDRYL GROUPS IN YEAST CELLS

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Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent.

Studies of protein-bound (PB-SH) and nonprotein bound sulfhydryl group (NP-SH) concentrations in tissues under various conditions is a prerequisite to understanding the role of sulfhydryls in living organisms. Many methods have been developed for the measurement of sulfhydryl groups, but these have been concerned chiefly only with the estimation of NP-SH in biological fluids or total SH groups ...

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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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Sulfhydryl Groups in Films of Egg Albumin

1. The same number of SH groups reduces ferricyanide in surface films of egg albumin as in albumin denatured by urea, guanidine hydrochloride, Duponol, or heat, provided the ferricyanide reacts with films while they still are at the surface and with the denatured proteins while the denaturing agent (urea, heat, etc.) is present. 2. The SH groups of a suspension of egg albumin made by clumping t...

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Distribution of Protein-bound Hexosamine in Chloroplasts.

Intact chloroplasts of spinach (Spinacia oleracea L.), sunflower (Helianthus annuus L.), and maize (Zea mays L.) mesophyll cells contained 0.33, 0.50, and 0.14% of bound hexosamine on a protein basis, respectively. Undifferentiated maize chloroplasts contained 0.19%. Values for chloroplast lamellae were, respectively, 0.16, 0.18, 0.12, and 0.06% and for envelope membranes they were 1.6, 2.5, 3....

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The reaction of methyl mercury nitrate with the sulfhydryl groups of yeast glyceraldehyde-3-phosphate dehydrogenase.

The importance of two of the thiol groups of yeast triosephosphate dehydrogenase for its activity haa been shown by the abolition of activity and diphosphopyridine nucleotide binding by the addition of 2 equivalents of p-chloromercuribenzoate (PCMB) (1, 2). The reaction of methyl mercury nitrate with this enzyme has been found to be anomalous in the sense that this mercury compound, unlike PCMB...

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ژورنال

عنوان ژورنال: Journal of Histochemistry & Cytochemistry

سال: 1962

ISSN: 0022-1554,1551-5044

DOI: 10.1177/10.5.568