Section 44
Chapter 43,147

Formation of alpha-1,2- and alpha-1,3-linked mannose disaccharides from mannosyl retinyl phosphate by rat liver membrane enzymes

Quill, H.; Wolf, G.

Annals of the new York Academy of Sciences 359: 331-344


ISSN/ISBN: 0077-8923
PMID: 6942679
DOI: 10.1111/j.1749-6632.1981.tb12758.x
Accession: 043146932

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Mannosyl retinyl phosphate (MRP) was an active substrate for the transfer of mannose to methyl-alpha-D-mannose (CH3-alpha-man), p-nitrophenyl-alpha-D-mannose, and free mannose. The products formed during MRP incubation with CH3-alpha-man or with mannose were alpha-linked. The disaccharides formed by incubation of MRP with mannose were identified by paper chromatography and electrophoresis as mannose-alpha-1,2-mannose and mannose-alpha-1,3-mannose. Triton X-100 greatly inhibited mannose-alpha-1,3-mannose synthesis. In the absence of detergent, MnCl2, NiCl2, and ZnCl2 inhibited synthesis of both products. Formation of mannose-alpha-1,3-mannose was more sensitive to preincubation of the enzyme at 40 degrees C then was synthesis of mannose-alpha-1,2-mannose. No differences in membrane mannosyltransferase activity with MRP, compared to DMP, could be demonstrated.

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