Catalytic center of lecithin:cholesterol acyltransferase: isolation and sequence of diisopropyl fluorophosphate-labeled peptides
Lecithin:cholesterol acyltransferase (LCAT) was purified from hog plasma and subsequently reacted with (/sup 3/H)-Diisopropyl fluorophosphate (DFP). The labeled enzyme was digested with pepsin and the peptides separated by high performance liquid chromatography (HPLC). Two radioactive peptides were isolated, subjected to automated amino acid sequencing and yielded the following data: A) Ile-Ser-Leu-Gly-Ala-Pro-Trp-Gly-Gly-Ser, and B) Tyr-Ile-Phe-Asp-x-Gly-Phe-Pro-Tyr-x-Asp-Pro-Val. Both of these sequences represent very highly conserved regions of the enzyme when compared to the sequence of human LCAT. Peptide (A) is considered to represent the catalytic center of LCAT based on comparisons with data reported in the literature.
- Research Organization:
- North Texas State Univ., Forth Worth
- OSTI ID:
- 6576972
- Journal Information:
- Biochem. Biophys. Res. Commun.; (United States), Vol. 1
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
PEPTIDES
AMINO ACID SEQUENCE
TRANSFERASES
FRACTIONATION
LIQUID COLUMN CHROMATOGRAPHY
SWINE
TRACER TECHNIQUES
TRITIUM COMPOUNDS
ANIMALS
CHROMATOGRAPHY
DOMESTIC ANIMALS
ENZYMES
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MAMMALS
MOLECULAR STRUCTURE
ORGANIC COMPOUNDS
PROTEINS
SEPARATION PROCESSES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques