D
David Kobylka
Researcher at Oklahoma State University–Stillwater
Publications - 8
Citations - 377
David Kobylka is an academic researcher from Oklahoma State University–Stillwater. The author has contributed to research in topics: Membrane protein & Membrane. The author has an hindex of 7, co-authored 8 publications receiving 376 citations.
Papers
More filters
Journal ArticleDOI
Proteins and glycoproteins of the erythrocyte membrane.
TL;DR: Molecular weights of glycoproteins calculated from acrylamide gel electrophoresis were found to vary with the percentage of acrieslamide in the gel, indicating that these proteins do not behave in a normal fashion in this electrophoreis system.
Journal ArticleDOI
Proteins and glycoproteins of the milk fat globule membrane
David Kobylka,Kermit L. Carraway +1 more
TL;DR: By examination of a number of membrane samples, it was shown that the major protein and the major glycoprotein are the most invariant components in terms of percentage composition over a series of preparations.
Journal ArticleDOI
Surface proteins of erythrocyte membranes.
TL;DR: Diazotized sulfanilic acid labeling and trypsin digestion studies of human and bovine erythrocytes indicate that the glycoprotein of each species is the only major membrane protein which is readily accessible at the cell surface.
Journal ArticleDOI
Proteolytic digestion of proteins of the milk fat globule membrane.
David Kobylka,Kermit L. Carraway +1 more
TL;DR: Results indicate that the membrane surrounding the fat globule does not represent a significant permeability barrier to proteolytic enzymes and suggest that the membranes does not exist in an intact form on the globule.
Journal ArticleDOI
Chemical modification of erythrocyte membranes: double labeling with acetic anhydride.
TL;DR: The results of the double labeling procedure suggest that the structure of the membrane of the intact cell may be different from that of the isolated ghost and that caution must be exercised in deducing membrane structure solely from studies of isolated membranes.