Identification of proapoa-I in rat lymph and plasma: Metabolic conversion to "mature" apoA-I

Giancarlo Ghiselli, William A. Bradley, Antonio Gotto, Bette C. Sherrill

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Rat apoA-I polymorphism has been analyzed in lymph and plasma. Two major proteins were present and their relative distribution was different in lymph and plasma lipoproteins. The basic protein (pI 5.60) was quantitatively most abundant among plasma lipoproteins and the acidic protein (pI 5.50) was predominant in lymph chylomicrons and lipoproteins. Microsequence amino acid analysis of the two proteins isolated by preparative isoelectrofocusing revealed that pI 5.50 apoA-I was proapoA-I with six additional amino acids (H2N-Ser-Glu-Phe-Trp-Gln-Gln) at the N-terminal end of "mature" apoA-I (pI 5.60 apoA-I). When radioiodinated proapoA-I was injected in rats, a conversion to "mature" apoA-I was observed and the process reached 92% completion in six hours. These data demonstrate the origin of apoA-I polymorphism in vivo.

Original languageEnglish (US)
Pages (from-to)704-711
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume116
Issue number2
DOIs
StatePublished - Oct 31 1983

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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