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Multiple forms of the proline-rich polypeptide (PRP) bound to rat prostatic binding protein
Biochemical and Biophysical Research Communications
|February 28, 1983
Summary
Rat prostatic binding protein contains heterogeneous proline-rich polypeptides (PRP). Six distinct PRP forms were isolated, differing in size and amino acid composition, revealing complex protein variations.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Proline-rich polypeptide (PRP) bound to rat prostatic binding protein exhibits heterogeneity.
- This heterogeneity is observed consistently across different rat strains.
Purpose of the Study:
- To characterize the different forms of PRP.
- To investigate the structural variations within PRP.
Main Methods:
- Isoelectric focusing to assess heterogeneity.
- Carboxymethylcellulose chromatography for separation of PRP forms.
- Molecular weight determination.
- Amino acid composition analysis.
Main Results:
- Isoelectric focusing revealed major PRP bands at pH 7.6 and pH 6.9.
- Carboxymethylcellulose chromatography separated six distinct PRP forms.
- Five forms (MW: 4000) share N- and C-terminal amino acids (glycine and lysine) but differ in internal amino acid substitutions.
- A sixth form (MW: 3500) has a truncated N-terminus.
Conclusions:
- Rat PRP is a complex mixture of related polypeptides.
- Structural variations include differences in size and internal amino acid sequences.
- These findings contribute to understanding protein diversity in rat prostate.