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Enzymatic, isoelectric, and molecular‐weight characterization of water‐soluble maize‐pollen proteins
Author(s) -
ORTEGA E. I.,
BATES L. S.
Publication year - 1980
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1980.tb03270.x
Subject(s) - isoelectric point , isoelectric focusing , esterase , biochemistry , enzyme , polyacrylamide gel electrophoresis , molecular mass , chromatography , chemistry , aminopeptidase , peroxidase , biology , leucine , amino acid
Maize ( Zea mays L. cv. Kansas Drought Synthetic) pollen proteins were fractionated via a continuous tandem cascade ultrafiltration system into three molecular‐weight classes. Proteins from the whole extract and each fraction were further separated by polyacrylamide gel electrofocusing in the pH 5 to 9 range and characterized by their enzymatic activity and isoelectric point. Twenty‐one protein bands were detected with Fast Green FCF staining. Esterase, peroxidase, leucine aminopeptidase, catalase, and amylase activities were located in 16 bands. Five bands remained unclassified. All the enzymes assayed, except amylase, were polymorphic. The extractions, fractionations and zymograms were reproducible and indicated that several protein bands contained at least two different enzymes with very similar molecular weight class and isoelectric point for each enzyme and protein band