The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Purification and Properties of the Components from Troponin
Open accessAbstract
Procedures have been developed for purification of three of the four protein components usually found in skeletal muscle troponin preparations. These three components are the ones required for troponin activity, and an apparent functional property of each has been defined. TN-I with a molecular weight of 24,000 inhibits actomyosin ATPase activity both in the presence and absence of Ca++. TN-T, with a molecular weight of 37,000, interacts with tropomyosin as evidenced by the appearance of a new hypersharp peak when mixtures of the two proteins are examined in the analytical ultracentrifuge. TN-C, with a molecular weight of 20,000, was the only component which possesses high affinity Ca++ binding activity. The sulfhydryl groups of troponin are found only in TN-I and TN-C. TN-I and TN-T require salt for full solubility and both proteins show a strong tendency to aggregate. An attempt has been made to interpret results on troponin fractionation obtained in other laboratories in the light of the properties of our purified components.
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Cites
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THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
Scatchard, G. (1949) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1949.tb27297.x · Cited by 19,778
DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTION
Gornall, A. G., Bardawill, C. J., & David, M. M. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)57021-6 · Cited by 16,158
Estimation of the molecular weights of proteins by Sephadex gel-filtration
Andrews, P. (1964) · Biochemical Journal · doi:10.1042/bj0910222 · Cited by 3,899
Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
Shapiro, A. L., Viñuela, E., & V. Maizel, J. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(67)90391-9 · Cited by 3,763
Spectroscopic Determination of Tryptophan and Tyrosine in Proteins*
Edelhoch, H. (1967) · Biochemistry · doi:10.1021/bi00859a010 · Cited by 3,436
On the Determination of Cystine as Cysteic Acid
Moore, S. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83985-6 · Cited by 3,012
Calcium and muscle contraction
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Cited by
Potter, J. D., & Gergely, J. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41347-1 · Cited by 916
Self-citationCardiac troponins: from myocardial infarction to chronic disease
Park, K. C., Gaze, D. C., Collinson, P. O., & Marber, M. S. (2017) · Cardiovascular Research · doi:10.1093/cvr/cvx183 · Cited by 510
Katrukha, A. G., Bereznikova, A. V., Esakova, T. V., Pettersson, K., Lövgren, T., Severina, M. E., Pulkki, K., Vuopio-Pulkki, L.-M., & Gusev, N. B. (1997) · Clinical Chemistry · doi:10.1093/clinchem/43.8.1379 · Cited by 266
Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range
Thomas, D. D., Seidel, J. C., & Gergely, J. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90259-6 · Cited by 137
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Metadata
- Authors
- Greaser, M. L., & Gergely, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1973-03
- Volume
- 248
- Issue
- 6
- Pages
- 2125-2133
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1495195805
- Cited by
- 332
- References
- 21
- FWCI
- 16.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
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