The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
A Form of Cytochrome b 5 That Contains an Additional Hydrophobic Sequence of 40 Amino Acid Residues
Open accessAbstract
A species of cytochrome b 5 with a monomer molecular weight of 16,700 has been isolated from rabbit-liver microsomes by a procedure that uses detergents and avoids the use of any proteolytic or lipolytic enzymes. This detergent-extracted cytochrome b 5 is larger than the trypsin- or lipase-extracted enzyme, and appears to contain an extremely hydrophobic appendage of 40 amino acids, probably at the N-terminus. The hydrophobic character of the extra amino acid sequence leads to aggregation in the absence of detergents, and may be of considerable importance in the binding of the enzyme to microsomes. It is suggested that the hydrophilic portion of the cytochrome molecule, which bears the heme and is enzymatically functional, is oriented toward the surface of the membrane where it readily reacts with nonmicrosomal proteins, while the hydrophobic “tail” anchors the heme protein tightly to the membrane.
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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
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 20,298
DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*
Davis, B. J. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14213.x · Cited by 18,892
Spectroscopic Determination of Tryptophan and Tyrosine in Proteins*
Edelhoch, H. (1967) · Biochemistry · doi:10.1021/bi00859a010 · Cited by 3,436
Equilibrium Ultracentrifugation of Dilute Solutions*
Yphantis, D. A. (1964) · Biochemistry · doi:10.1021/bi00891a003 · Cited by 3,384
Reynolds, J. A., & Tanford, C. (1970) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.66.3.1002 · Cited by 695
Turnover of Constituents of the Endoplasmic Reticulum Membranes of Rat Hepatocytes
Omura, T., Siekevitz, P., & Palade, G. E. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95974-0 · Cited by 483
The Purification And Properties Of Microsomal Cytochrome Reductase
Strittmatter, P., & Velick, S. F. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70660-1 · Cited by 218
Self-citationPurification by Means of Detergents and Properties of Cytochrome b5 from Liver Microsomes
Ito, A., & Sato, R. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93204-7 · Cited by 184
The Nature of the Heme Binding in Microsomal Cytochrome b5
Strittmatter, P. (1960) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64647-2 · Cited by 113
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Cited by
The Hydrophobic Effect and the Organization of Living Matter
Tanford, C. (1978) · Science · doi:10.1126/science.653353 · Cited by 985
DESATURATION AND RELATED MODIFICATIONS OF FATTY ACIDS
Shanklin, J., & Cahoon, E. B. (1998) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.49.1.611 · Cited by 916
Nuclear matrix: isolation and characterization of a framework structure from rat liver nuclei
Berezney, R., & Coffey, D. (1977) · The Journal of Cell Biology · doi:10.1083/jcb.73.3.616 · Cited by 587
Membrane Receptors and Hormone Action
Cuatrecasas, P., & Hollenberg, M. D. (1976) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60481-7 · Cited by 478
Parkos, C. A., Allen, R. A., Cochrane, C. G., & Jesaitis, A. J. (1987) · Journal of Clinical Investigation · doi:10.1172/jci113128 · Cited by 455
Metadata
- Authors
- Spatz, L., & Strittmatter, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1971-05
- Volume
- 68
- Issue
- 5
- Pages
- 1042-1046
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2083008862
- Cited by
- 455
- References
- 11
- FWCI
- 8.44
- Type
- journal article
- Language
- en
- Open access
- green
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- Spatz, L., & Strittmatter, P. (1971). A Form of Cytochrome b 5 That Contains an Additional Hydrophobic Sequence of 40 Amino Acid Residues. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.68.5.1042
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
