Fluorescence of 2-hydroxy-3-naphthoic acid hydrazide derivatives of side-chain carboxyl groups of proteins |
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Authors: | Dr. Sherill K. Curtis Prof. Ronald R. Cowden |
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Affiliation: | (1) University of Denver, Denver, Colorado, USA;(2) Present address: Department of Anatomy, Albany Medical College, 12208 Albany, N.Y., USA |
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Abstract: | Summary Sections processed through the first part of the Barrnett and Seligman (1958) procedure, which is considered to be selective for side-chain carboxyl groups of proteins, are fluorescent when exposed to incident blue light. The results of a number of tests suggest that the fluorescence can be ascribed principally to binding of 2-hydroxy-3-naphthoic acid hydrazide (HNAH) by mixed acid anhydride derivatives of side-chain carboxyl groups of proteins. Thus, the procedure appears to be a fluorescent counterpart of the bright-field method of Barrnett and Seligman. |
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