AbstractMyosin subfragment-1 (S-1), digested with trypsin in the presence of ATP, rapidly loses its ATPase activity upon mild heat treatment even if ATP or ADP is present. The heat-treated molecule is very sensitive to further tryptic digestion. Undigested S-1 and S-1 digested in the absence of ATP are protected by nucleotides. The loss of the protective effect of nucleotides correlates with the tryptic splitting of the 25 kDa aminoterminal fragment between Arg 23 and Ile 24
AbstractThe ATP-induced dissociation of actoS1 has been studied at temperatures between −10°C and +3...
AbstractOn binding to myosin subfragment 1 (S1), the γ-amido derivative of ATP (ATPγNH2), an isomer ...
The amounts of ATP and ADP bound to myosin during the ATPase reaction [EC 3.6.1.3] were determined i...
AbstractMyosin subfragment-1 (S-1), digested with trypsin in the presence of ATP, rapidly loses its ...
AbstractThe influence of adenine nucleotides and Mg2+ on the thermal denaturation of mitochondrial F...
The tryptophan fluorescence of unmodified myosin subfragment 1 (S1) from rabbit and chicken skeletal...
AbstractThe thermal denaturation of the myosin subfragment 1 (S1) from rabbit skeletal muscle and of...
AbstractThe structure of the myosin subfragment-1 (SI) from rabbit skeletal muscle was studied using...
The yield of S-l** * from tryptic digests of HMM was 65%. The sa> w value of S-l •was 5.03 S at a...
Low concentrations of p-chloromercuribenzoate (PCMB), Zn++, or Cd++ increase the ATPase and CTPase a...
AbstractWe applied different methods, such as turbidity measurements, dynamic light scattering, diff...
Skeletal muscle myosin is an enzyme that interacts allosterically with MgATP and actin to transduce ...
<div><p>Myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (...
AbstractThe reaction of trypsin on the heavy chain of gizzard myosin and chymotryptic HMM was invest...
Enzymatic properties of heavy meromyosin (HMM) were studied using ribose 5'-triphosphate (RTP) ...
AbstractThe ATP-induced dissociation of actoS1 has been studied at temperatures between −10°C and +3...
AbstractOn binding to myosin subfragment 1 (S1), the γ-amido derivative of ATP (ATPγNH2), an isomer ...
The amounts of ATP and ADP bound to myosin during the ATPase reaction [EC 3.6.1.3] were determined i...
AbstractMyosin subfragment-1 (S-1), digested with trypsin in the presence of ATP, rapidly loses its ...
AbstractThe influence of adenine nucleotides and Mg2+ on the thermal denaturation of mitochondrial F...
The tryptophan fluorescence of unmodified myosin subfragment 1 (S1) from rabbit and chicken skeletal...
AbstractThe thermal denaturation of the myosin subfragment 1 (S1) from rabbit skeletal muscle and of...
AbstractThe structure of the myosin subfragment-1 (SI) from rabbit skeletal muscle was studied using...
The yield of S-l** * from tryptic digests of HMM was 65%. The sa> w value of S-l •was 5.03 S at a...
Low concentrations of p-chloromercuribenzoate (PCMB), Zn++, or Cd++ increase the ATPase and CTPase a...
AbstractWe applied different methods, such as turbidity measurements, dynamic light scattering, diff...
Skeletal muscle myosin is an enzyme that interacts allosterically with MgATP and actin to transduce ...
<div><p>Myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (...
AbstractThe reaction of trypsin on the heavy chain of gizzard myosin and chymotryptic HMM was invest...
Enzymatic properties of heavy meromyosin (HMM) were studied using ribose 5'-triphosphate (RTP) ...
AbstractThe ATP-induced dissociation of actoS1 has been studied at temperatures between −10°C and +3...
AbstractOn binding to myosin subfragment 1 (S1), the γ-amido derivative of ATP (ATPγNH2), an isomer ...
The amounts of ATP and ADP bound to myosin during the ATPase reaction [EC 3.6.1.3] were determined i...