scholarly journals The primary structure of troponin T and the interaction with tropomyosin

1975 ◽  
Vol 151 (1) ◽  
pp. 85-97 ◽  
Author(s):  
P Jackson ◽  
G W Amphlett ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Troponin T ◽  
Troponin C ◽  
The Other ◽  
Tryptic Digestion ◽  
Partial Digestion ◽  
Common Sequence

1. Eight peptides were separated from the CNBr digest of troponin T from rabbit white skeletal muscle and characterized. 2. By study of the amino acid sequence of the methionine-containing peptides isolated after chymotryptic and tryptic digestion and of the N- and C-terminals of the CNBr peptides, six of the latter were shown to be arranged in the sequence CNB1-CNB2-CNB5-CNB6-CNB8-CNB7. The other two peptides, CNB1′ and CNB3, have been shown to be partial digestion products. 3. The CNBr peptides CNB1′ and CNB2 contained a common sequence and were the only peptides in CNBr digests of troponin T that formed a complex with tropomyosin as judged by viscometric and electrophoretic studies. 4. It is concluded that tropomyosin interacts with the N-terminal half of the troponin T molecule approximately in the region lying between residues 70 and 160. 5. Electrophoretic evidence indicates that tropomyosin and troponin C interact with troponin T. 6. None of the major CNBr peptides of troponin T isolated formed a complex with troponin C on electrophoresis at pH 8.6.

The binding sites of rabbit skeletal troponin-I on troponin-T

1980 ◽  
Vol 58 (8) ◽  
pp. 649-654 ◽  
Author(s):  
Joyce R. Pearlstone ◽  
Lawrence B. Smillie
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Site ◽  
Binding Sites ◽  
Troponin I ◽  
Troponin T ◽  
Gel Filtration ◽  
Troponin C ◽  
Separate Site

Various fragments derived from rabbit skeletal muscle troponin-T (Tn-T) by chemical and (or) proteolytic cleavage were mixed with whole troponin-I (Tn-I) and applied to a Sephadex G-75 gel filtration column in order to determine the binding site of Tn-I on Tn-T. This site of interaction was found to span two distinct regions of Tn-T. The first site involves the highly acidic NH2-terminal fragment CB3 (residues 1–70 of Tn-T). A second separate site is located in the region of residues 152–209 of Tn-T. The present study, in conjunction with our earlier work on tropomyosin – Tn-T binding and Tn-T – troponin-C binding, depicts Tn-T as being a functionally efficient molecule composed of several distinct domains of specialized amino acid sequence, each of which carries out a role in the binding of a different protein.

scholarly journals Characterization of a Novel Thrombin-like Enzyme, Globlase from the Venom of Gloydius blomhoffii (Japanese Mamushi)

2019 ◽  
pp. 1-8
Author(s):  
Yumiko Komori ◽  
Yusuke Takashima ◽  
Shoko Ono ◽  
Toshiaki Nikai
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Isoelectric Point ◽  
Primary Structure ◽  
Polyacrylamide Gel Electrophoresis ◽  
Hydrolytic Activity ◽  
The Other ◽  
Clotting Factor ◽  
Human Fibrinogen

Aims: To elucidate the coagulation mechanisms of a novel clotting factor isolated from Gloydius blomhoffii venom, its hydrolytic activity on various substrates were examined. Furthermore the primary structure was determined and compared with the other snake venom components. Methodology: A thrombin-like enzyme was isolated from the crude venom of G. blomhoffii by DE52 Cellulose and CM52 Cellulose column chromatography. Enzyme activity was measured by using synthetic substrates (arginine esters, MCA-substrates and 3-(Acyloxy)-4-nitrobenzoic acid). Effect on fibrinogen was detected with bovine and human fibrinogen. Isoelectric point and molecular mass were measured by polyacrylamide gel electrophoresis and MALDI-TOF-MS. Amino acid sequence was decided with a protein sequencer by analyzing enzymatically cleaved peptides. Results: A clotting factor was found to be homologous as indicated by a single band on SDS-PAGE, and the final preparation was named as globlase. Molecular mass of this enzyme was determined to be 13,876.36 Da and the isoelectric point was 8.8. Globlase showed arginine ester hydrolytic activity, and specificity for substrates of thrombin. Proteolytic activity and phospholipase A2 (PLA2) activity were not detected. Complete amino acid sequence analysis indicated that the primary structure of globlase is similar to PLA2. However the aspartic acid which exists in the active site of PLA2 was found to be substituted by glutamine. Conclusion: It was shown in our current investigation that globlase is a novel thrombin-like enzyme isolated from G. blomhoffii venom. It was revealed that this enzyme had structure unlike the serine-protease such as the other thrombin-like enzymes.

The Amino-Acid Sequence of Troponin C from Frog Skeletal Muscle

1978 ◽  
Vol 91 (1) ◽  
pp. 231-242 ◽  
Author(s):  
Jean-Paul EERD ◽  
Jean-Paul CAPONY ◽  
Conception FERRAZ ◽  
Jean-Francois PECHERE
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Troponin C ◽  
Frog Skeletal Muscle

scholarly journals The amino-acid sequence of troponin C from frog skeletal muscle

1978 ◽  
Vol 91 (1) ◽  
pp. 239-242
Author(s):  
Jean-Paul Eerd ◽  
Jean-Paul Capony ◽  
Conception Ferraz ◽  
Jean-Francois Pechere
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Troponin C ◽  
Frog Skeletal Muscle

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

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