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Heterogeneity in buffalo lutropin.
K Muralidhar1, T Rajendrakumar, H P Sharma
1Department of Zoology, University of Delhi.
Indian Journal of Biochemistry & Biophysics
|April 1, 1992
Summary
Water buffalo lutropin (LH) shows variations in its alpha-subunit, indicating multiple forms. Different purification methods yield distinct buffalo LH preparations with unique properties.
Area of Science:
- Reproductive biology
- Protein chemistry
- Comparative endocrinology
Background:
- Lutropin (LH) is a crucial reproductive hormone.
- Microheterogeneity in protein structure can affect biological function.
- Previous studies suggested potential variations in buffalo LH.
Purpose of the Study:
- To investigate the microheterogeneity of water buffalo lutropin (LH).
- To compare different preparations of buffalo LH obtained through distinct purification protocols.
- To identify potential multiple forms of buffalo LH.
Main Methods:
- Analysis of N-terminal amino-acid sequences of LH subunits.
- Physicochemical characterization of LH preparations, including subunit dissociation, sugar composition, isoelectric point, and S-200 elution profiles.
- Comparative analysis of two distinct buffalo LH preparations (bu LH-1 and bu LH-2).
Main Results:
- Microheterogeneity was observed in the N-terminal amino-acid sequence of the alpha-subunit of buffalo LH (bu LH-1).
- The beta-subunit of buffalo LH did not exhibit microheterogeneity.
- A second purification protocol yielded buffalo LH (bu LH-2) with different physicochemical properties compared to bu LH-1, suggesting distinct forms.
Conclusions:
- The findings indicate the presence of more than one form of lutropin in water buffaloes.
- Microheterogeneity in the alpha-subunit contributes to the observed variations in buffalo LH.
- Different purification strategies can isolate distinct buffalo LH variants with unique characteristics.