Identification of proapoa-I in rat lymph and plasma: metabolic conversion to "mature" apoA-I. Academic Article uri icon

Overview

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.

publication date

  • October 31, 1983

Research

keywords

  • Apolipoproteins
  • Apolipoproteins A
  • Lymph
  • Protein Precursors

Identity

Scopus Document Identifier

  • 0021032581

Digital Object Identifier (DOI)

  • 10.1016/0006-291x(83)90582-x

PubMed ID

  • 6418165

Additional Document Info

volume

  • 116

issue

  • 2