Identification of water-soluble proteases in myelin preparations.
Sodium chloride extracts obtained from purified bovine brain myelin were found to contain proteolytic activity capable of degrading isolated myelin basic protein as assessed by SDS gel electrophoresis. Using gels copolymerized with gelatin as substrate, two bands at about 54 and 117-125 KDa, respectively, were detected. Activity corresponding to the 54 KDa band was inhibited by zinc. Data presented in this article suggest that proteolytic activity can be released from the myelin sheath in water-soluble form and recognize MBP as substrate.
Liuzzi
G M
GM
Dipartimento di Biochimica e Biologia Molecolare, Universita di Bari, Italy.
Ventola
A
A
Riccio
P
P
Quagliariello
E
E
D000818:Animals; D001921:Brain / Q000201:enzymology* / Q000648:ultrastructure; D002417:Cattle; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D004676:Myelin Basic Protein / Q000302:isolation & purification / Q000378:metabolism*; D009186:Myelin Sheath / Q000201:enzymology* / Q000648:ultrastructure
D004676:Myelin Basic Protein; D010450:Endopeptidases