跳轉至內容
Merck
  • Glycosidase activity in the post-ecdysial cuticle of the blue crab, Callinectes sapidus.

Glycosidase activity in the post-ecdysial cuticle of the blue crab, Callinectes sapidus.

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology (2001-04-06)
R D Roer, K E Halbrook, T H Shafer
摘要

We have previously demonstrated a marked change in sugar moieties of glycoproteins of the cuticle of the blue crab, Callinectes sapidus, between 0.5 and 3 h post-ecdysis. The present study has identified a glycosidase that appears in the cuticle during the early post-ecdysial hours. The enzyme has affinities for p-nitrophenyl derivatives of both N-acetylglucosamine and N-acetylgalactosamine. Both activities are competitively inhibited by chitobiose, suggesting that the enzyme could be a N-acetylhexosaminidase (EC 3.2.1.52). Atypical of N-acetylhexosaminidases described to date, this enzyme has a pH optimum of 7.0. The enzyme activity is high during the post-ecdysial period coincident with the changes in glycoprotein profiles observed in vivo. Partial purification of the enzyme has been accomplished by Sephacryl size-exclusion chromatography followed by concanavalin A affinity chromatography.

材料
產品編號
品牌
產品描述

Sigma-Aldrich
4-硝基苯基-N-乙酰-β-D-半乳糖胺, ≥98%
Sigma-Aldrich
4-Nitrophenyl N-acetyl-α-D-galactosaminide, substrate for N-acetyl-α-D-galactosaminidase