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- W2000736184 abstract "5 min of tryptic digestion of purified rabbit skeletal α-actinin decreases by approximately 75% the ability of α-actinin to cross-link F-actin filaments as measured viscometrically at 27°C, but has little effect on the sedimentation coefficient of α-actinin at 20°C or on α-actinin's ability to increase the Mg2+-modified ATPase activity and rate of turbidity increase of reconstituted actomyosin suspensions. Twenty to sixty min of trypsin treatment reduces the sedimentation coefficient of α-actinin and destroys much of α-actinin's ability to increase the Mg2+-modified ATPase and rate of turbidity increase of reconstituted actomyosin suspensions. Therefore the ability of α-actinin to increase the rate of in vitro measures of muscle contraction may not result directly from α-actinin's ability to cross-link F-actin filaments. Trypsin does not split α-actinin into large fragments as it does myosin. Previous studies have shown that 35 to 65% of total tryptic-susceptible peptide bonds in α-actinin are split after 60 min of incubation with trypsin and that 30% of these bonds split in 60 min are cleaved during the first 5 min in a rapid reaction. That splitting of this group of peptide bonds has little effect on the sedimentation coefficient of α-actinin indicates that these bonds are located in a region of the α-actinin molecule where noncovalent forces are strong enough to maintain conformation of the native α-actinin molecule even after these bonds have been split. This ostensible segregation of α-actinin's ability to cross-link F-actin filaments from its ability to increase rate of in vitro assays of contraction by tryptic digestion may suggest that α-actinin could have at least two different physiological roles: (1) to bind actin filaments to each other or to basal structures, and (2) to enhance the effectiveness of actin in supporting movement." @default.
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- W2000736184 title "Effect of trypsin on rabbit skeletal muscle α-actinin" @default.
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- W2000736184 doi "https://doi.org/10.1016/0005-2795(76)90010-6" @default.
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