Preferential tritium labelling of binding site residues in alpha chymotrypsin by exposure of the 1,3-3H-diisopropylphosphoryl derivative to tritiated hydrogen sulfide-Reference-Cited by-同舟云学术

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Preferential tritium labelling of binding site residues in alpha chymotrypsin by exposure of the 1,3-3H-diisopropylphosphoryl derivative to tritiated hydrogen sulfide

Published:1975 Issue:1 Volume:11 Page:11-20
ISSN:0022-2135
Container-title:Journal of Labelled Compounds
language:en
Short-container-title:J. Labelled Cpd. Radiopharm.

Author:

White Frederick H.

Publisher

Wiley

Subject

Organic Chemistry,Spectroscopy,Drug Discovery,Radiology, Nuclear Medicine and imaging,General Medicine,Biochemistry,Analytical Chemistry,Organic Chemistry,Spectroscopy,Drug Discovery,Radiology, Nuclear Medicine and imaging,Biochemistry,Analytical Chemistry

Reference12 articles.

1. Free-Radical Distributions in Several Gamma-Irradiated Dry Proteins as Determined by the Free-Radical Interceptor Technique

2. Comparison of Electrical Discharge with γ-Radiation for the Production of Free Radicals in Lyophilized Proteins

3. Radical Distributions in γ-Irradiated Dry Proteins at 195°K

4. - in Methods in Enzymol., Vol. 25, Part B, p. 387, Ed. by and ., Academic Press, Inc., New York, 1964.

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