Beta-N-acetyl-D-glucosaminidase multiple forms isolated from calf rennet

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State: Public
Version: author
Serval ID
serval:BIB_347EB17DD99D
Type
Inproceedings: an article in a conference proceedings.
Publication sub-type
Abstract (Abstract): shot summary in a article that contain essentials elements presented during a scientific conference, lecture or from a poster.
Collection
Publications
Institution
Title
Beta-N-acetyl-D-glucosaminidase multiple forms isolated from calf rennet
Title of the conference
3rd Joint Meeting of the Biochemical Societies of France, Germany and Switzerland
Author(s)
Persico M., Widmer F.
Address
Basel, Switzerland, September 30-October 2, 1985
ISBN
0177-3593
Publication state
Published
Issued date
1985
Peer-reviewed
Oui
Volume
366
Series
Biological Chemistry Hoppe-Seyler
Pages
834
Language
english
Abstract
The occurrence of lysozyme activity in calf rennet and abomasal fluid has recently been reported. In addition, ß-N-acetyl-D-hexosaminidase activity (Mr ca. 80'000) was also detected in the course of the purification procedure used for this lysozyme. We now report the isolation of four multiple molecular forms exhibiting ß-N-acetyl-D-glucosaminidase activity (EC 3.2.1.30). In addition to their in vivo physiological role, such enzymes could be useful for the structural analysis of various glycoproteins.
Crude calf rennet was used as the starting material, and the purification steps included precipitation in the presence of ammonium sulfate, gel filtration, cation and anion exchange chromatography. The ß-N-acetyl-D-hexosaminidase activity was tested at the various purification steps with the following substrates: 4-nitrophenyl-2-acetamido-2-deoxy-ß-D-glucopyranoside, 4-nitrophenyl-2-acetamido-2-deoxy-ß-D-galactopyranoside, colloidal chitin and chitobiose.
The four isolated enzyme forms were most active when hydrolyzing the synthetic glucosaminide substrate, and three of them also hydrolyzed the galactosaminide substrate (relative reaction rate: ca. 13%). By contrast, no significant endo-chitinase activity could be detected, whereas chitobiose was susceptible to enzymatic hydrolysis. The isolated enzyme forms thus appear to act preferentially on low Mr substrates.
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20/08/2019 14:21
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