The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Ribonuclease inhibitor from human placenta. Purification and properties.
Open accessAbstract
A soluble ribonuclease inhibitor from the human placenta has been purified 4000-fold by a combination of ion exchange and affinity chromatography. The inhibitor has been isolated in 45% yield (about 2 mg/placenta) as a protein that is homogeneous by sodium dodecyl sulfate-gel electrophoresis. In common with the inhibitors of pancreatic ribonuclease from other tissues that have been studied earlier, the placental inhibitor is an acidic protein of molecular weight near 50,000; it forms a 1:1 complex with bovine pancreatic RNase A and is a noncompetitive inhibitor of the pancreatic enzyme, with a Ki of 3 X 10(-10) M. The amino acid composition of the protein has been determined. The protein contains 30 half-cystine plus cysteine residues determined as cysteic acid after performic acid oxidation. At pH 8.6 the nondenatured protein alkylated with iodoacetic acid in the presence of free thiol has 8 free sulfhydryl groups. The inhibitor is irreversibly inactivated by sulfhydryl reagents and also by removal of free thiol from solutions of the protein. Inactivation by sulfhydryl reagents causes the dissociation of the RNase - inhibitor complex into active RNase and inactive inhibitor.
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Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 317,331
Colorimetric Method for Determination of Sugars and Related Substances
DuBois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., & Smith, F. (1956) · Analytical Chemistry · doi:10.1021/ac60111a017 · Cited by 52,269
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 20,298
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
Self-citation[117] Chromatographic determination of amino acids by the use of automatic recording equipment
Moore, S., & Stein, W. H. (1963) · Methods in Enzymology · doi:10.1016/0076-6879(63)06257-1 · Cited by 1,696
Self-citation[37] Reaction of protein sulfhydryl groups with Ellman's reagent
Habeeb, A. F. S. A. (1972) · Methods in Enzymology · doi:10.1016/s0076-6879(72)25041-8 · Cited by 901
Amino Acid Analysis: Aqueous Dimethyl Sulfoxide As Solvent for the Ninhydrin Reaction
Moore, S. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94488-1 · Cited by 832
Self-citationHugli, T. E., & Moore, S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45285-x · Cited by 595
Self-citationSTUDIES ON THE GROSS STRUCTURE, CROSS-LINKAGES, AND TERMINAL SEQUENCES IN RIBONUCLEASE
Anfinsen, C. B., Redfield, R. R., Choate, W. L., Page, J., & Carroll, W. R. (1954) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71260-x · Cited by 431
[6] Topics in the methodology of substitution reactions with agarose
Parikh, I., March, S., & Cuatrecasas, P. (1974) · Methods in Enzymology · doi:10.1016/s0076-6879(74)34009-8 · Cited by 220
Cited by
Characterization of the ribonuclease activity on the skin surface
Probst, J., Brechtel, S., Scheel, B., Hoerr, I., Jung, G., Rammensee, H.-G., & Pascolo, S. (2006) · Genetic Vaccines and Therapy · doi:10.1186/1479-0556-4-4 · Cited by 84
Metadata
- Authors
- Blackburn, P., Wilson, G., & Moore, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1977-08
- Volume
- 252
- Issue
- 16
- Pages
- 5904-5910
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1584133579
- Cited by
- 271
- References
- 15
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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