Proteolysis of spectrin by trypsin and pronase in the presence of phospholipid suspensions.
The effect of phospholipid suspensions on the proteolysis of isolated spectrin was examined by SDS-polyacrylamide gradient gel electrophoresis. Proteolysis of spectrin in the membranes by trypsin and pronase was also studied. It was found that electrophoretic patterns of spectrin fragments were influenced by the presence of the suspension prepared from phosphatidylethanolamine:phosphatidylserine (60:40) mixture and of phosphatidylcholine. Qualitative changes in the proteolytic patterns obtained after proteolysis of spectrin by pronase in the presence of phosphatidylcholine suspension were observed. The changes in the sensitivity of spectrin towards proteases result probably from changes in the accessibility of some peptide bonds upon the interaction of this extrinsic protein with phospholipids.
Sikorski
A F
AF
Institute of Biochemistry, Wrocław University, Poland.
Kozubek
A
A
Szopa
J
J
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D010455:Peptides / Q000032:analysis; D010743:Phospholipids / Q000378:metabolism*; D011402:Pronase / Q000378:metabolism*; D051381:Rats; D013049:Spectrin / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism*
D010455:Peptides; D010743:Phospholipids; D013049:Spectrin; D014357:Trypsin; D011402:Pronase