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Tissue‐specific variation of pea mitochondrial polypeptides detected by computerized image analysis of two‐dimensional electrophoresis gels
Author(s) -
HumpherySmith Ian,
des FrancsSmall Catherine Colas,
AmbartBretteville Françoise,
Remy René
Publication year - 1992
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150130134
Subject(s) - etiolation , pisum , mitochondrion , biochemistry , biology , polyacrylamide gel electrophoresis , electrophoresis , gel electrophoresis , botany , chemistry , enzyme
A tissue‐specific variation of a total of 152 mitochondria‐associated polypeptides is detailed for etiolated leaves, epicotyls and roots from the pea, Pisum satisum L., using computerized image analysis. These organ systems possess, respectively, 128, 100, and 96 mitochondria‐associated polypeptides with 38, 8, and 10, respectively, being unique to each. Seventy‐one polypeptides were observed to be present in all gels, but some of these also underwent a variety of quantifiable changes. Two polypeptides were identified that varied similarly to a polypeptide of interest (W), known to be abundant in pea epicotyls and potato tubers. It is postulated that these latter three polypeptides are therefore probably related functionally.