Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.454238
Title: A biochemical study of the surface of an adhesive variant of BHK21 cells
Author: Dysart, Jean McKinlay
ISNI:       0000 0001 3436 7247
Awarding Body: University of Glasgow
Current Institution: University of Glasgow
Date of Award: 1975
Availability of Full Text:
Access from EThOS:
Access from Institution:
Abstract:
A variant of BHK 21/C13 cells, which arose spontaneously in culture, was isolated and cloned. The aggregative behaviour of the variant was studied by means of a reciprocating shaker/electronic particle counting technique and found to differ from that of the parent line. Freshly trypsinized C13 cells aggregate rapidly at 37°C while the variant and a polyoma virus transformed derivative show little aggregation after forty minutes. Neither neuraminidase nor dibutyryl cyclic AMP increased the aggregation of the variant to the level attained by C13 cells. When the variant cells were removed from the culture flasks by ethylene-diamine-tetra-acetic acid (EDTA), rather than trypsin, they aggregated in a manner similar to C13 cells while the transformed derivative still showed little aggregation. The variant had a lower sialyl transferase aotlvity towards endogenous acceptors but the same activity towards exogenous acceptors as C13 cells. The cells were also assayed for galactosyl transferase activity and no differences were found between the variant and the parent line. Isolated plasma membranes were also assayed and again no differences were found. The proteins of the isolated plasma membranes were analysed by polyacrylamide gel electrophoresis. Two proteins of estimated molecular weights 182,000 and 47,500 were absent from the membranes of polyoma virus transformed cells. These same two proteins were released from C13 and the variant cell membranes by mild trypsinization. The possible role of these proteins in cell adhesion is discussed.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.454238  DOI: Not available
Share: