The DOI matches its Crossref record.
Acetylation of human serum albumin by p-nitrophenyl acetate
Abstract
Human serum albumin reacts very rapidly with p-nitrophenyl acetate (NphOAc). Rapid acetylation of the protein accompanies and largely accounts for the easily observed rapid formation of of p-nitrophenolate ion. One group is acetylated much faster than all others. It appears to be located in a high affinity binding site for small fatty acid anions, to have a pKa of 8.7, and a limiting bimolecular rate of reaction with NphOAc of approximately 3 X 10(4) M-1 sec-1 at alkaline pH values. Rapid reversible binding appears to be a major contributor to the high reaction velocity.
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Cited by
Enzyme promiscuity: evolutionary and mechanistic aspects
Khersonsky, O., Roodveldt, C., & Tawfik, D. S. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.08.011 · Cited by 641
Metadata
- Authors
- Means, G. E., & Bender, M. L.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1975-11-04
- Volume
- 14
- Issue
- 22
- Pages
- 4989-4994
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2088222952
- Cited by
- 168
- References
- 0
- FWCI
- 0.55
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Acetylation of human serum albumin by p-nitrophenyl acetate. https://app.cochat.ai/papers/10.1021/bi00693a031
- The paper
- Means, G. E., & Bender, M. L. (1975). Acetylation of human serum albumin by p-nitrophenyl acetate. Biochemistry. https://doi.org/10.1021/bi00693a031
Data sources
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.
