Proteins Released from Myofibrils by CASF (Ca2+-activated sarcoplasmic factor) and Trypsin |
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Authors: | Atsushi Suzuki Yoshinobu Nonami Darrel E Goll |
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Institution: | 1. Department of Animal Science, Faculty of Agriculture, The University of Niigata, Niigata, Japan;2. Departments of Animal Science and of Biochemistry and Biophysics, Iowa State University, Ames, Iowa 50010, U.S.A. |
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Abstract: | The nature of the soluble proteins and peptides released from myofibrils by treatment with CASF (Ca2+-activated sarcoplasmic factor) was investigated by using Polyacrylamide gel electrophoresis in both a nondenaturing and a denaturing (sodium dodecyl sulfate=SDS) solvent and by using gel permeation chromatography on Sepharose 6B. Both CASF and trypsin treatment cause removal of Z-disks before causing other ultrastructurally detectable degradation of myofibrils. CASF treatment of myofibrils releases a protein that is identical to α-actinin, one of the known components of the Z-disk, on the basis of mobility in Polyacrylamide gel electrophoresis in a nondenaturing solvent and in SDS and on the basis of elution from gel permeation columns. Trypsin treatment of myofibrils releases a number of smaller molecular weight products that cannot be identified with any of the known myofibrillar proteins. Hence, CASF seems to remove Z-disks from myofibrils by means of a very specific proteolytic activity that releases α-actinin without extensively degrading it. Trypsin, on the other hand, probably seems to remove Z-disks by degrading α-actinin to peptides. |
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Keywords: | dextran sulfate sodium-induced colitis dipeptidyl peptidase IV glucagon-like peptide-2 organic acid |
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