Amino acid composition and proteolytic generated domains of higher plant tubulin.
The molecular architecture of tubulin from higher plant remains unknown. In this report we have made an attempt to identify higher plant tubulin domains using total and limited proteolysis of Haemanthus endosperm tubulin. The tubulin was previously purified and characterized (Picquot and Lambert 1988). The amino acid composition revealed a high content of basic residues, such as arginine and lysine. Tubulin domains were probed by tryptic and chymotryptic cleavage and analyzed by immunoblotting using specific monoclonal antibodies against alpha or beta subunits. These data shed light on specific properties of the higher plant tubulin.
Picquot
P
P
Laboratoire de Biologie Cellulaire Végétale, Centre National de la Recherche Scientifique, Unité Associée 1182, Université Louis Pasteur, Strasbourg, France.
Vantard
M
M
Amiri
I
I
Fausser
L
L
Lambert
A M
AM
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002918:Chymotrypsin; D015151:Immunoblotting; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D010944:Plants / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D013552:Swine; D014357:Trypsin; D014404:Tubulin / Q000235:genetics* / Q000302:isolation & purification
D000596:Amino Acids; D046911:Macromolecular Substances; D010446:Peptide Fragments; D014404:Tubulin; D002918:Chymotrypsin; D014357:Trypsin