Studies on prolactin 48: isolation and properties of the hormone from horse pituitary glands.
Abstract: Isolation of prolactin from equine pituitary glands has been described. It has a potency of 42 IU/mg in the pigeon crop-sac test and consists of 199 amino acids. The hormone has only four half-cystine residues in contrast to other mammalian prolactins which have six residues. From NH2-terminal sequence analysis and amino acid composition of cyanogen bromide fragments, the NH2-terminal disulfide loop is missing in the equine prolactin molecule. Circular dichroism spectra indicate that the alpha-helical content of equine prolactin appears to be lower (50%) than that found in the ovine hormone (65%).
Publication Date: 1983-01-01 PubMed ID: 6830233DOI: 10.1016/0003-9861(83)90402-2Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The research article discusses the extraction of a hormone called prolactin from the pituitary gland of a horse, examines its potency, and analyzes its structure, comparing it to that of prolactin from other mammals.
Research Methodology and Findings
- The researchers started by isolating prolactin from the pituitary glands of horses.
- The isolated hormone showed a potency of 42 International Units per milligram when tested in the pigeon crop-sac test. This test is a standard assay for prolactin activity.
- The prolactin hormone was found to be made up of 199 amino acids.
Comparison with Other Mammalian Prolactin
- The structure of the equine prolactin was unique compared to prolactin molecules found in other mammals. Specifically, equine prolactin only contained four half-cystine residues. These residues are typically involved in forming disulfide bonds that stabilize the protein’s structure.
- However, other mammalian prolactins usually have six such residues, suggesting a different structure in the equine prolactin molecule.
Structural Analysis
- The structure of the equine prolactin molecule was further investigated using NH2-terminal sequence analysis and examination of amino acid composition of cyanogen bromide fragments.
- These tests revealed the absence of the NH2-terminal disulfide loop in the equine prolactin, another structural difference from other mammalian prolactins.
- Furthermore, circular dichroism spectra indicated that the alpha-helical content of equine prolactin (a measure of its structural complexity) is lower (50%) than that of prolactin from sheep (65%). This suggests that the equine hormone may have a less complex, and perhaps less stable, structure than the ovine version of the hormone.
Conclusion
- The research provides important insights into the unique properties and structure of equine prolactin. The observed differences in structure could potentially affect how the hormone functions. However, further exploration would be required to understand the full implications of these variations.
Cite This Article
APA
Li CH, Chung D.
(1983).
Studies on prolactin 48: isolation and properties of the hormone from horse pituitary glands.
Arch Biochem Biophys, 220(1), 208-213.
https://doi.org/10.1016/0003-9861(83)90402-2 Publication
Researcher Affiliations
MeSH Terms
- Amino Acids / analysis
- Animals
- Chemical Phenomena
- Chemistry
- Chromatography, Gel
- Horses
- Pituitary Gland / analysis
- Prolactin / isolation & purification
Grant Funding
- AM-6097 / NIADDK NIH HHS
Citations
This article has been cited 2 times.- Butnev VY, Gotschall RR, Baker VL, Moore WT, Gout PW, Bousfield GR. Glycosylated equine prolactin and its carbohydrate moiety. J Protein Chem 1996 Jul;15(5):413-26.
- Miller JL, Reddy A, Harman RM, Van de Walle GR. A xenotransplantation mouse model to study physiology of the mammary gland from large mammals. PLoS One 2024;19(2):e0298390.
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