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The Primary Structure of the Phosphatidylcholine-Exchange Protein from Bovine Liver.
- Source :
- European Journal of Biochemistry; 5/12/80, Vol. 106 Issue 1, p279-290, 12p
- Publication Year :
- 1980
-
Abstract
- The phosphatidylcholine exchange protein from bovine liver consists of a single polypeptide chain and has a blocked N terminus. The protein contains an estimated 244 amino acid residues in accordance with a determined molecular weight of 28 000. The protease from mouse submaxillaris gland cleaved the citraconylated and S-carboxymethylated derivative of the exchange protein at one specific site (Arg<superscript>14</superscript>-Glu<superscript>15</superscript>) close to the N terminus. Analysis of the two resulting peptides showed that N-acetyl-methionine was the N-terminal residue and gave the sequence of the first 41 residues. The modified protein was also fragmented with the protease from Staphylococcus aureus. The peptides isolated represented 88% of the protein; their sequences were determined by manual and automated Edman degradation. Alignment of a number of these peptides gave the complete sequence of the N-terminal half up to position 122. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 106
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13488302
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1980.tb06020.x