Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide.
In myofibrils, titin (also called connectin) molecules span from Z line to M line and constitute a third filament system containing an elastic domain in the I band. This giant protein is particularly sensitive to proteolysis in situ. Treatment of rabbit skeletal myofibrils with exogenous proteinases induces a release of titin fragments, which are detected in the soluble myofibrillar fraction. The cleavage of titin occurs at specific points localized at the proximity of Z line and could lead to a concomitant release of alpha-actinin.
Astier
C
C
Centre de Recherches de Biochimie Macromoléculaire LP 9008 (C.N.R.S.), Université Montpellier I, France.
Labbé
J P
JP
Roustan
C
C
Benyamin
Y
Y
D000818:Animals; D015153:Blotting, Western; D064211:Connectin; D010450:Endopeptidases / Q000378:metabolism*; D015151:Immunoblotting; D008970:Molecular Weight; D009124:Muscle Proteins / Q000302:isolation & purification / Q000378:metabolism*; D009210:Myofibrils / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism*; D011494:Protein Kinases; D011817:Rabbits; D012697:Serine Endopeptidases / Q000378:metabolism; D014108:Tosylphenylalanyl Chloromethyl Ketone / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism
D064211:Connectin; D009124:Muscle Proteins; D010446:Peptide Fragments; D014108:Tosylphenylalanyl Chloromethyl Ketone; D011494:Protein Kinases; D010450:Endopeptidases; C044499:submandibular proteinase A; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin