AbstractLimited proteolysis of actin with trypsin removes its two or three C-terminal amino acid residues [Proc. Natl. Acad. Sci. USA 81 (1984) 3680–3684]. Carboxypeptidase B-treatment of G- and F-actin previously digested with trypsin revealed that in the first case preferential release of three and in the second two C-terminal amino acid residues takes place. Tryptic removal of three but not two C-terminal amino acid residues of actin causes weakening of its interaction with caldesmon and lowering of the caldesmon-induced inhibitory effect on actomyosin ATPase activity. Therefore, it is concluded that the third amino acid residue from the C terminus of actin, Lys-373, is important for the interaction with caldesmon
An attempt to develop a short and reliable method of caldesmon purification led to the development o...
AbstractWe have investigated the functional properties of a mutant (Cg1) derived from the C-terminal...
AbstractThe regulatory system of smooth muscle thin filaments is thought to involve a major calcium-...
AbstractLimited proteolysis of actin with trypsin removes its two or three C-terminal amino acid res...
AbstractProteolytic elimination of three C-terminal amino acid residues from actin weakens its inter...
Caldesmon interacts with the NH2-terminal region of actin. It is now shown in airfuge centrifugation...
The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of ...
AbstractLimted proteolysis of caldesmon has been used in studying the structure-function relationshi...
AbstractDigestion of caldesmon with carboxypeptidase Y is accompanied by loss of its ability to inhi...
Cleavage of caldesmon with chymotrypsin yields a series of fragments which bind both calmodulin and ...
Caldesmon (CaD) is known as an actin binding protein. In this study, we proposed that a trace amount...
AbstractCaldesmon is an actin- and myosin-binding protein found in smooth muscle that inhibits actin...
The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of ...
AbstractCaldesmon was stoichiometrically N-carbethoxylated specifically at the only histidine residu...
The time course of interaction of caldesmon with actin may be monitored by fluorescence changes that...
An attempt to develop a short and reliable method of caldesmon purification led to the development o...
AbstractWe have investigated the functional properties of a mutant (Cg1) derived from the C-terminal...
AbstractThe regulatory system of smooth muscle thin filaments is thought to involve a major calcium-...
AbstractLimited proteolysis of actin with trypsin removes its two or three C-terminal amino acid res...
AbstractProteolytic elimination of three C-terminal amino acid residues from actin weakens its inter...
Caldesmon interacts with the NH2-terminal region of actin. It is now shown in airfuge centrifugation...
The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of ...
AbstractLimted proteolysis of caldesmon has been used in studying the structure-function relationshi...
AbstractDigestion of caldesmon with carboxypeptidase Y is accompanied by loss of its ability to inhi...
Cleavage of caldesmon with chymotrypsin yields a series of fragments which bind both calmodulin and ...
Caldesmon (CaD) is known as an actin binding protein. In this study, we proposed that a trace amount...
AbstractCaldesmon is an actin- and myosin-binding protein found in smooth muscle that inhibits actin...
The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of ...
AbstractCaldesmon was stoichiometrically N-carbethoxylated specifically at the only histidine residu...
The time course of interaction of caldesmon with actin may be monitored by fluorescence changes that...
An attempt to develop a short and reliable method of caldesmon purification led to the development o...
AbstractWe have investigated the functional properties of a mutant (Cg1) derived from the C-terminal...
AbstractThe regulatory system of smooth muscle thin filaments is thought to involve a major calcium-...