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Multiple forms of N-acetyl-β-hexosaminidase in developing tadpole fins

✍ Scribed by Stuart, Elizabeth S. ;Everett, Gale Beliveau ;Fischer, Mark S.

Book ID: 102893512
Publisher: John Wiley and Sons
Year: 1978
Tongue: English
Weight: 508 KB
Volume: 205
Category: Article
ISSN: 0022-104X
DOI: 10.1002/jez.1402050209

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✦ Synopsis

Abstract

The degradative enzyme N‐acetyl‐β‐D‐hexosaminidase (Hex) (E.C. 3.2.1.30) has been isolated from livers and tail fins of the amphibian R. catesbeiana. Two amphibian hexosaminidases have been resolved by polyacrylamide gel electrophoresis and quantitated by assay of the separated forms. The electrophoretic mobilities of the hexosaminidases were the same whether isolated from liver or tail tissue. The ratio of hexosaminidase enzymes is constant and independent of developmental stage, tissue source, or method of preparation. It has been concluded that tail resorption and increases in Hex activity are not initiated by changes in the ratio of enzymes and that the net affect of any changes in protein synthesis and degradation must leave the ratio of forms unaltered.

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