Abstract: | The use of galactose oxidase (EC 1.1.3.9) and tritiated sodium borohydride for labeling of membrane glycoproteins, described by Gahmberg and Hakomori2, has previously been applied to the study of myelin glycoproteins of experimental animals8. Rat brain myelin glycoproteins have been studied by sequential lectin affinity chromatography12 and recently the lectin-binding capacity of rat central nervous system myelin glycoproteins has been characterized7. Complex heterogeneity of the glycoprotein pattern of rat central nervous system myelin has been reported7,8,12, and so a variety of glycoproteins can be expected to exist in human white matter membranes. Application of the galactose oxidase procedure to the study of human brain membranes could be useful in research concerning certain neurological diseases if the properties of autopsy brain material are taken into account. In this study, membrane proteins of human autopsy brain white matter were subjected to the galactose oxidase/NaB3H4 labeling procedure and the membranes labeled by this method or by the 3H]acetic anhydride techniques6 were studied by lectin affinity chromatography using Lens culinaris phytohemagglutinin (lentil lectin) attached to Sepharose 4B beads. |