The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Multiple Forms of Human Glutathione S‐Transferase and Their Affinity for Bilirubin
Open accessAbstract
The initial enzymic step in mercapturic acid formation is catalyzed by glutathione S‐transferase. Several species of this enzyme, designated as transferases α. β, γ, δ and e an the basis of increasing isoelectric points, were isolated from human liver. Evidence is presented that each of the purified species is homogeneous with respect to sodium dodecylsulfate‐gel electrophoresis. Transferases α, β and ɛ each appear as a single band an gel electrofocusing: transferases α and δ are present as two and three bands, respectively, with each band catalytically active. Amino acid analysis indicated the five transferases to be either very closely related or identical in this respect. All enzyme species have a molecular weight of about 48 500 and consist of two apparently identical subunits. The spectrum of substrates is the same for each although the enzymes differ slightly in specific activity. As is the case for the rat liver enzymes, each of the human transferases binds bilirubin although this compound is not a substrate
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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
Habig, W. H., Pabst, M. J., & Jakoby, W. B. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42083-8 · Cited by 18,221
Self-citationLITWACK, G., KETTERER, B., & ARIAS, I. M. (1971) · Nature · doi:10.1038/234466a0 · Cited by 575
Self-citationThe Identity of Glutathione S -Transferase B with Ligandin, a Major Binding Protein of Liver
Habig, W. H., Pabst, M. J., Fleischner, G., Gatmaitan, Z., Arias, I. M., & Jakoby, W. B. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.10.3879 · Cited by 539
Self-citationWrigley, C. W. (1971) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(71)22040-1 · Cited by 305
Robinson, A. B., McKerrow, J. H., & Cary, P. (1970) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.66.3.753 · Cited by 261
Reyes, H., Levi, A. J., Gatmaitan, Z., & Arias, I. M. (1971) · Journal of Clinical Investigation · doi:10.1172/jci106721 · Cited by 209
Self-citationCuatrecasas, P., & Illiano, G. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(71)80175-4 · Cited by 137
Multiple Forms of Cytochrome c in the Rat
Flatmark, T., & Sletten, K. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93588-x · Cited by 123
Cited by
[51] Assays for differentiation of glutathione S-Transferases
Habig, W. H., & Jakoby, W. B. (1981) · Methods in Enzymology · doi:10.1016/s0076-6879(81)77053-8 · Cited by 2,419
Self-citationGlutathione Transferases—Structure and Catalytic Activit
Mannervik, B., Helena Danielson, U., & Ketterer, B. (1988) · Critical Reviews in Biochemistry · doi:10.3109/10409238809088226 · Cited by 1,756
(1979) · Advances in Cancer Research · doi:10.1016/s0065-230x(08)60848-9 · Cited by 1,163
Mechanism for the several activities of the glutathione S-transferases.
Keen, J. H., Habig, W. H., & Jakoby, W. B. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)81842-0 · Cited by 757
Self-citationThe Glutathione S ‐Transferases: A Group of Multifunctional Detoxification Proteins
Jakoby, W. B. (1978) · Advances in Enzymology - and Related Areas of Molecular Biology · doi:10.1002/9780470122914.ch6 · Cited by 686
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Metadata
- Authors
- KAMISAKA, K., HABIG, W. H., KETLEY, J. N., ARIAS, I. M., & JAKOBY, W. B.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1975-12
- Volume
- 60
- Issue
- 1
- Pages
- 153-161
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2040930057
- Cited by
- 280
- References
- 12
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Open access
- bronze
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- KAMISAKA, K., HABIG, W. H., KETLEY, J. N., ARIAS, I. M., & JAKOBY, W. B. (1975). Multiple Forms of Human Glutathione S‐Transferase and Their Affinity for Bilirubin. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1975.tb20987.x
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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.
