Lipoprotein lipase cofactor activity of a carboxyl-terminal peptide of apolipoprotein C-II
| Autor: | Thomas A. Musliner, Eve C. Church, Marguerite J. Kingston, Peter N. Herbert, Richard S. Shulman |
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| Rok vydání: | 1977 |
| Předmět: |
chemistry.chemical_classification
Lipoprotein lipase Multidisciplinary Apolipoprotein B biology Apolipoprotein C-II Peptide Cofactor Enzyme Activation Kinetics Lipoprotein Lipase Structure-Activity Relationship Residue (chemistry) Succinylation Apolipoproteins Biochemistry chemistry biology.protein lipids (amino acids peptides and proteins) Amino Acid Sequence Peptides Peptide sequence Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 74:5358-5362 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.74.12.5358 |
| Popis: | Apolipoprotein C-II (apoC-II) is a small protein found associated with the plasma lipoproteins. It serves a unique function in the activation of the enzyme lipoprotein lipase (triacylglycerol acyl-hydrolase, EC 3.1.1.3). ApoC-II contains a single arginine residue, permitting tryptic cleavage into two peptides after succinylation of the native protein. The succinylated amino-terminal peptide, approximately 50 residues, did not activate lipoprotein lipase. The succinylated carboxyl-terminal peptide, about 29 residues, had significant cofactor activity. Relative to native apoC-II, the maximal activation observed with the succinylated carboxyl-terminal peptide was 50% lower and the concentration required for half-maximal activity was approximately 10 times higher. Mixtures of the carboxyl- and amino-terminal peptides had no more activity than the carboxyl-terminal peptide alone. Localization of functional properties to the carboxyl region is a feature also common to apolipoproteins C-III, A-II, and A-I. |
| Databáze: | OpenAIRE |
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