Mueller, Wolfgang and Haindl, Markus and Holler, Eggehard (2008) Physarum polymalic acid hydrolase: Recombinant expression and enzyme activation. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 377 (3). pp. 735-740. ISSN 0006-291X, 1090-2104
Full text not available from this repository. (Request a copy)Abstract
As a platform for syntheses of nanoconjugates in antitumor drug delivery, polymalic acid together with its tailoring specific exohydrolase is purified from plasmodium Cultures of the slime mold Physarum polycephalum, a member of the phylum myxomycota. Polymalic acid hydrolase is expressed in an inactive form that functions as a molecular adapter for polymalic acid trafficking within the plasmodium and is activated only during secretion. Activation follows specific protein tyrosine phosphorylation and dissociation from plasma membranes. Purified inactive Physarum polymalic acid hydrolase, recombinantly expressed in yeast Saccharomyces, is activated on a preparative basis by the addition of plasma membrane fragments from plasmodia of P. polycephalum. Activation of polymalic acid hydrolase and inhibition of polymalic acid synthesis by protein tyrosine phosphorylation are complementary events and could indicate a joint signal response to plasma membrane damage. (C) 2008 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DNA-POLYMERASE-ALPHA; SLIME-MOLD; POLYCEPHALUM; BETA-POLY(L-MALATE); PLASMODIA; POLY(BETA-L-MALATE); PROTEINS; CYCLE; Recombinant expression in Escherichia coli and yeast; Glycosylation; Zymogen; Hydrolase activation by phosphorylation; Plasma membrane protein tyrosine kinase; Secretion; Membrane damage; Plasmodium physiology; Biotechnology; Nanoconjugates |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eggehard Holler |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Oct 2020 08:47 |
| Last Modified: | 14 Oct 2020 08:47 |
| URI: | https://pred.uni-regensburg.de/id/eprint/29924 |
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