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https://doi.org/10.1016/S1357-2725(98)00057-0
DC Field | Value | |
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dc.title | Functional role of glycosylation on the recombinant CD38/ADP-ribosyl cyclase in CHO cells | |
dc.contributor.author | Chidambaram, N. | |
dc.contributor.author | Chang, C.F. | |
dc.date.accessioned | 2013-06-05T09:47:34Z | |
dc.date.available | 2013-06-05T09:47:34Z | |
dc.date.issued | 1998 | |
dc.identifier.citation | Chidambaram, N., Chang, C.F. (1998). Functional role of glycosylation on the recombinant CD38/ADP-ribosyl cyclase in CHO cells. International Journal of Biochemistry and Cell Biology 30 (9) : 1011-1018. ScholarBank@NUS Repository. https://doi.org/10.1016/S1357-2725(98)00057-0 | |
dc.identifier.issn | 13572725 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/38180 | |
dc.description.abstract | Current evidence suggests that CD38, a lymphocyte differentiation antigen, has been found to be functionally indistinguishable from the native form when it was expressed as a soluble and non-glycosylated protein in yeast. Studies were conducted to evaluate the functional role of glycosylation on the membrane-bound CD38 in mammalian cells. The stable transformants of CHO cells were established with pXJ41-CD38 construct and the recombinant CD38 was detected at the surface of CHO cells using a polyclonal antibody to rat CD38 by immunocytochemistry. The recombinant protein displaying ADP-ribosyl cyclase activity was purified from CHO cells, which appeared as 42 and 46 kDa bands on immunoblot under non-reducing and reducing conditions, respectively. The recombinant CD38 was then subjected to deglycosylation with N-glycosidase F that resulted in a 33 kDa band on immunoblot under reducing condition. Further the partial deglycosylation of the recombinant CD38, performed at various time intervals, resulted in a series of bands (33-46 kDa) on immunoblot. Kinetic analysis indicated that deglycosylation of the recombinant CD38 showed a considerable decrease in V(max) and an increase in K(m) of ADP-ribosyl cyclase activity. These observations clearly suggest that glycosylation plays an important role to maintain the enzymatic activity and substrate affinity of CD38/ADP-ribosyl cyclase for mediating the signalling events in mammalian cells. Copyright (C) 1998 Elsevier Science Ltd. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S1357-2725(98)00057-0 | |
dc.source | Scopus | |
dc.subject | ADP-ribosyl cyclase | |
dc.subject | CD38 | |
dc.subject | CHO cells | |
dc.subject | deglycosylation | |
dc.subject | enzyme kinetics | |
dc.type | Article | |
dc.contributor.department | BIOCHEMISTRY | |
dc.description.doi | 10.1016/S1357-2725(98)00057-0 | |
dc.description.sourcetitle | International Journal of Biochemistry and Cell Biology | |
dc.description.volume | 30 | |
dc.description.issue | 9 | |
dc.description.page | 1011-1018 | |
dc.description.coden | IJBBF | |
dc.identifier.isiut | 000076097700008 | |
Appears in Collections: | Staff Publications |
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