The amino acid sequence and structural class of the arachin subunit of molecular weight 29, 100A.
Arachin subunit (mol. wt. 29,100) from peanut of variety G-201 was separated and isolated, its purity and homogeneity were ascertained. The subunit was cleaved with trypsin, chymotrypsin and Staphylococcus aureus V8 protease. The fragments obtained were separated and isolated by PAGE, gel filtration & ion exchange chromatography, these were subjected to amino acid analysis, and Edman degradation. The PTH amino acids obtained were identified by spectroscopy and TLC. The complete amino acid sequence of the subunit (226 residues) was established, and the structural class of arachin was predicted from the amino acid composition.
Bhushan
R
R
Department of Chemistry, University of Roorkee, India.
Mahesh
V K
VK
Varma
A
A
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D010367:Arachis / Q000737:chemistry*; D002918:Chymotrypsin / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009943:Organophosphorus Compounds / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D017510:Protein Folding; D012697:Serine Endopeptidases / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
C043517:2-(4-isothiocyanatophenoxy)-1,3,2-dioxaphosphinene 2-oxide; D000596:Amino Acids; D009943:Organophosphorus Compounds; D010446:Peptide Fragments; D010940:Plant Proteins; C000102:Arachin; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C028344:glutamyl endopeptidase; D014357:Trypsin