Dissociation of light chains from cardiac myosin.
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Adenosine Triphosphatases↗
Biomedical subjects
F Fábián
Publications and source records attributed to F Fábián.
Isolation of the C-terminal peptides of rabbit skeletal myosin.
Purified LMM and its tryptic fragments (LF-1, LF-2 and LF-3) were treated with carboxypeptidase-A and the liberated amino acids were identified by thin layer ion-exchange charomatography. In each protein the only detectable amino acid was leucine. From the total tryptic digest of LMM the C-terminal leucine containing peptides were isolated. Two peptides were found with the following amino acid composition: asx1, g1x6, ala1, leu3, and g1n2-3, leu1, respectively. We obtained the same two peptides from the total tryptic digest of LF-3. We conclude that the C-terminal amino acid of the myosin heavy chain is leucine rather than isoleucine as suggested earlier. Heterogeneity of isolated C-terminal peptides might indicate a heterogeneity in the myosin heavy chains.
Amino Acid Sequence↗
18O-exchange catalyzed by myosin, heavy meromyosin, heavy meromyosin subfragment 1 and their complexes with actin.
Myosin, HMM and HMM S1 catalyze 18O-exchange between P1 and H218O of the medium at an intermediate stage of ATP hydrolysis ("intermediate 18O-exchange") in the presence of Mg2+. Natural complexes of actomyosin and acto-HMM S1 do not catalyze intermediate 18O-exchange but facilitate "direct" or "medium" 18O-exchange (KH2P18O4 in equilibrium H2O) even without ATP. Reconstituted complexes of actomyosin, acto-HMM, acto-HMM S1, PABC-HMM S1, congo-myosin and TNP-myosin do not catalyze direct 18O-exchange in the presence of Mg2+ and absence of ATP. From the data obtained a hypothetical sequence of phosphorylation and 18O-exchange reactions in myofibril action has been suggested.
Actins↗
Investigation of peptides containing half-cystine in pig pancreas amylase.
Sequence analysis of the carboxymethyl-cystein-containing tryptic peptides isolated after the total reduction and carboxymethylation of pig pancreas amylase has shown that the half-cystine-containing tryptic peptides of the isozymes have identical sequences. The fact that 10 tryptic peptides containing carboxymethyl-cystein could be isolated, supports the generally accepted view that pig pancreas amylase contains single polypeptide chain.
Amino Acid Sequence↗