PMID: 696476Jan 1, 1978Paper

The action of trypsin on central and peripheral nerve myelin

Advances in Experimental Medicine and Biology
E H Eylar, M W Roomi

Abstract

In contrast to other studies, our results demonstrate that low concentration of trypsin degrades a high proportion of proteolipid from CNS myelin. The Wolfgram protein and BP are vulnerable and completely lost on trypsinolysis, perhaps accounting for some of the peptides retained by the myelin. In PNS myelin, the major PO protein, a hydrophobic glycoprotein, is readily degraded to a stable 18,000--19,000 molecular weight unit, referred to as TPO protein, still retaining the carbohydrate unit which probably exists as a nonasaccharide grouping. Production of the TPO glycoprotein results from cleavage of a lysinyl-methionine or arginyl-methionine linkage probably found approximately 80--100 residues from the NH2-terminal isoleucine of the PO molecule. This linkage must be especially accessible to trypsin since the TPO protein is also generated in high yield when isolated PO protein is treated with trypsin in solution for 0.5 hours. Further incubation for 24 hours fully degrades the TPO protein to over 20 tryptic peptides, shown by peptide mapping, unlike the situation in myelin where the TPO unit is stable and resists further proteolysis. The TPO unit is also produced when PO protein is treated with BrCN. The PO protein contains 3...Continue Reading

Citations

Oct 1, 1982·Journal of Neurochemistry·R N RapaportR P Skoff
Apr 1, 1981·Journal of Neurochemistry·C Linington, T V Waehneldt
Sep 1, 1981·Journal of Neurochemistry·C Mezei, J A Verpoorte
Apr 1, 1979·Neurochemical Research·E H EylarS Greenfield
Oct 26, 2005·The Journal of Biological Chemistry·T Tristan BrandhorstBruce S Klein
Jul 1, 1981·Journal of Neurochemistry·R N Rapaport, J A Benjamins

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