PROTEOLYTIC DIGESTION OF BOVINE BRAIN WHITE MATTER PROTEOLIPID

PROTEOLYTIC DIGESTION OF BOVINE BRAIN WHITE MATTER PROTEOLIPID —Proteolipids were previously considered to be resistant to proteolytic digestion. In the present study, crude bovine white matter proteolipid, proteolipid apoprotein, and chemically modified proteolipids were subjected to the action of the following proteolytic enzymes in the absence and presence of detergents: trypsin, α‐chymotrypsin, elastase, thermolysin and collagenase. The course of digestion was followed by the release of Fluorescamine‐reactive groups. Tryptic digestion of the crude proteolipid and the apoprotein in the absence of detergent amounted to 10 and 40% respectively of the digestion in the presence of detergent. Peptide mapping and protein analyses of both the soluble digests and the insoluble residues confirmed digestion. In the presence of either sodium deoxycholate or Triton X‐100, essentially all of the crude proteolipid and 60% of the proteolipid apoprotein were solubilized by trypsin. Digestion of the apoprotein was observed only in preparations which had not been dried. In the absence of detergent, (1) the oxidized crude proteolipid was more susceptible to tryptic digestion than were either the unoxidized or carboxymethylated preparations, (2) both the apoprotein and the oxidized proteolipid were digested by thermolysin or α‐chymotrypsin, and (3) all preparations were attacked by elastase. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

PROTEOLYTIC DIGESTION OF BOVINE BRAIN WHITE MATTER PROTEOLIPID

Journal of Neurochemistry, Volume 25 (5) – Nov 1, 1975

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Publisher
Wiley
Copyright
Copyright © 1975 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-3042
eISSN
1471-4159
D.O.I.
10.1111/j.1471-4159.1975.tb04373.x
Publisher site
See Article on Publisher Site

Abstract

—Proteolipids were previously considered to be resistant to proteolytic digestion. In the present study, crude bovine white matter proteolipid, proteolipid apoprotein, and chemically modified proteolipids were subjected to the action of the following proteolytic enzymes in the absence and presence of detergents: trypsin, α‐chymotrypsin, elastase, thermolysin and collagenase. The course of digestion was followed by the release of Fluorescamine‐reactive groups. Tryptic digestion of the crude proteolipid and the apoprotein in the absence of detergent amounted to 10 and 40% respectively of the digestion in the presence of detergent. Peptide mapping and protein analyses of both the soluble digests and the insoluble residues confirmed digestion. In the presence of either sodium deoxycholate or Triton X‐100, essentially all of the crude proteolipid and 60% of the proteolipid apoprotein were solubilized by trypsin. Digestion of the apoprotein was observed only in preparations which had not been dried. In the absence of detergent, (1) the oxidized crude proteolipid was more susceptible to tryptic digestion than were either the unoxidized or carboxymethylated preparations, (2) both the apoprotein and the oxidized proteolipid were digested by thermolysin or α‐chymotrypsin, and (3) all preparations were attacked by elastase.

Journal

Journal of NeurochemistryWiley

Published: Nov 1, 1975

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