Title
Partial-purification and further characterization of the novel endoglucosaminidase from human serum that hydrolyzes 4-methylumbelliferyl-N-acetyl-<tex>$\beta$</tex>-D-chitotetraoside (MU-TACT hydrolase)
Author
Faculty/Department
Faculty of Medicine and Health Sciences
Publication type
article
Publication
Oxford ,
Subject
Chemistry
Biology
Source (journal)
The international journal of biochemistry. - Oxford, 1970 - 1994
Volume/pages
26(1994) :12 , p. 1369-1375
ISSN
0020-711X
ISI
A1994QD19700006
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
A novel endoglucosaminidase, originally described by Den Tandt et al. [Int. J. Biochem. 20 (1988), 713-719] and bearing the provisional name MU-TACT hydrolase, was purified from human serum 56,000-fold by means of ammonium sulphate precipitation, anion-exchange chromatography, Con A-Sepharose chromatography and gel filtration on Sepharose CL-6B followed by Superose 12 HR. Based on the latter technique the native apparent molecular weight of the enzyme appeared to be equal to that of myoglobin, being approx. 17 kD. The enzyme eluted clearly at a different volume than lysozyme. MU-TACT is a commercially available substrate for lysozyme. For unknown reasons two major peptides co-purify that give bands on SDS-PAGE of 55-60 and 31 kD, respectively.
E-info
https://repository.uantwerpen.be/docman/iruaauth/91e72e/a044338.pdf
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