Evidence for an increase in positive surface charge and an increase in susceptibility to trypsin of Sarcophaga lectin (from the flesh fly, Sarcophaga peregrina) on its interaction with galactose, a hapten sugar of the lectin.
When Sarcophaga lectin (from the flesh fly, Sarcophaga peregrina), an insect humoral lectin, was eluted from a column of DEAE-cellulose in the presence of galactose (a hapten sugar of this lectin), it emerged at a lower salt concentration than when galactose was absent. In the presence of galactose the lectin was, in addition, more susceptible to trypsin digestion. The lectin was found to have an affinity for basic proteins such as histone H3 and sarcotoxin IA, but this property was lost in the presence of galactose. These results suggested that the lectin changes its conformation on interaction with galactose. This change is suggested to result in the exposure of some hidden lysine and/or arginine residues.
Komano
H
H
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Kurama
T
T
Nagasawa
Y
Y
Natori
S
S
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D015152:Blotting, Northern; D004175:Diptera; D005690:Galactose / Q000378:metabolism*; D015870:Gene Expression; D006241:Haptens / Q000737:chemistry; D006657:Histones / Q000302:isolation & purification / Q000378:metabolism; D019476:Insect Proteins; D037102:Lectins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D037181:Lectins, C-Type; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D013499:Surface Properties; D014357:Trypsin / Q000378:metabolism*
C043030:20kDa lectin protein, Sarcophaga; D000596:Amino Acids; D006241:Haptens; D006657:Histones; D019476:Insect Proteins; D037102:Lectins; D037181:Lectins, C-Type; D046911:Macromolecular Substances; D014357:Trypsin; D005690:Galactose