Plant annexin form homodimer during Ca(2+)-dependent liposome aggregation

Biochem Mol Biol Int. 1995 Apr;35(4):749-55.

Abstract

The annexin (p35) was isolated from the fruits of green pepper (Capsicum annum). The partial amino acid sequence of p35 was analyzed. p35 had an endonexin fold as annexin consensus sequences. Purified p35 had other annexin like characters such as strongly bind to phosphatidylserine and phosphatidylinositol, phospholipase A2 inhibition and liposome aggregation. The zero-length crosslinking assay revealed that p35 formed a homodimer during Ca(2+)-dependent liposome aggregation.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Annexins / chemistry*
  • Annexins / genetics
  • Arabidopsis / genetics
  • Calcium-Binding Proteins / chemistry*
  • Calcium-Binding Proteins / genetics
  • Capsicum / genetics
  • Cattle
  • Consensus Sequence
  • Kinetics
  • Liposomes / chemistry*
  • Molecular Sequence Data
  • Phospholipases A / chemistry
  • Phospholipases A2
  • Phospholipids / chemistry
  • Plant Proteins, Dietary / chemistry*
  • Plants, Medicinal
  • Sequence Homology, Amino Acid
  • Swine

Substances

  • Annexins
  • Calcium-Binding Proteins
  • Liposomes
  • Phospholipids
  • Plant Proteins, Dietary
  • Phospholipases A
  • Phospholipases A2

Associated data

  • GENBANK/Z18518