Studies on the structure-function relationship of proteins, specifically of galactosyltransferases and their modifiers like alpha-lactalbumin, have been initiated. For such studies, we are producing the normal and altered proteins by the recombinant DNA methodology. A T7-promoter and a polylinker DNA sequence was inserted into a baculovirus vector adjacent to the polyhydrin promoter. Such constructs are used for the production of normal and altered proteins in, a) baculovirus infected insect cells, or b) frog oocytes by injecting the cDNA specific mRNA transcribed in vitro by T7-polymerase. We have also engineered the cDNA sequences of galactosyltransferase and alpha-lactalbumin, in such a way that the expression of the cDNA sequence have a potential to produce either soluble and secreted forms, or membrane anchored forms of the protein.
