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Human sperm protamines. Amino-acid sequences of two forms of protamine P2
Abstract
Human protamine P2 was purified to homogeneity by solubilizing whole spermatozoa in guanidinium X HCl containing 2-mercaptoethanol, alkylating the resulting protamine thiols with vinylpyridine, removing acid-insoluble material by acid dialysis and using CM-cellulose chromatography to remove non-protamine basic proteins and separate protamines P1 and P2. The P2 preparation contained two components, P2a and P2b, which were sequenced completely without being separated. The peptides obtained from thermolysin and endoproteinase Lys-C digestions were purified by reverse-phase high-pressure liquid chromatography and sequenced using a gas-phase sequencer. P2a contains 57 amino acids and has a relative molecular mass of 7636 while P2b contains 54 amino acids, which are identical to residues 4-57 of P2a, and has a relative molecular mass of 7242. Protamine P2a is approximately 50% homologous with human protamine P1. The amino acid sequence of P2a is: (sequence; see text)
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Cited by
Harford, C., & Sarkar, B. (1997) · Accounts of Chemical Research · doi:10.1021/ar9501535 · Cited by 508
Induction of oxidative DNA damage by carcinogenic metals
Bal, W., & Kasprzak, K. S. (2002) · Toxicology Letters · doi:10.1016/s0378-4274(01)00483-0 · Cited by 187
Metadata
- Authors
- McKAY, D. J., RENAUX, B. S., & DIXON, G. H.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1986-04
- Volume
- 156
- Issue
- 1
- Pages
- 5-8
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1597996421
- Cited by
- 169
- References
- 0
- FWCI
- 15.02
- Type
- journal article
- Language
- en
- Open access
- closed
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- McKAY, D. J., RENAUX, B. S., & DIXON, G. H. (1986). Human sperm protamines. Amino-acid sequences of two forms of protamine P2. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1986.tb09540.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.