Purification and N-terminal sequencing of style glycoproteins associated with self-incompatibility in Petunia hybrida.
We report isolation and N-terminal amino acid sequencing of three style glycoproteins, which segregate with three S (self-incompatibility) alleles of Petunia hybrida. The S-glycoproteins were expressed mainly in the upper part of the pistil and showed an increasing concentration during flower development. The glycoproteins were purified by a combination of ConA-Sepharose and cation exchange fast protein liquid chromatography. The amount of S-glycoproteins recovered from style extracts varied from 0.5 to 1.6 micrograms per style, which was 40-60% of the amount recovered by a simplified analytical method. N-terminal amino acid sequences of S1-, S2- and S3-glycoprotein showed homology within the fifteen amino terminal residues. These amino acid sequences were compared with the previously published sequences of S-glycoproteins from Nicotiana alata and Lycopersicon peruvianum.
Broothaerts
W J
WJ
Laboratory of Plant Physiology, Katholieke Universiteit Leuven, Belgium.
van Laere
A
A
Witters
R
R
Préaux
G
G
Decock
B
B
van Damme
J
J
Vendrig
J C
JC
D000483:Alleles; D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D014644:Genetic Variation; D006023:Glycoproteins / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D018521:Plant Physiological Phenomena; D010940:Plant Proteins / Q000235:genetics* / Q000302:isolation & purification; D010944:Plants / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D006023:Glycoproteins; D010940:Plant Proteins