Alternate enzymes for use in cholinesterase antagonist monitors : CAM's /

Mode of access: Internet.

CAM-4, a portable warning device for organophosphate hazardous material spills /

Mode of access: Internet.

Die design and construction; lanking, piercing, compound, progressive, trimming, flanging, forming, and cam dies.

Mode of access: Internet.

Dom Bento de Cam?oes e o principe dos poetas Lusitanos /

"Ediç?ao correcta e muito ampliadá dum artigo publicado no 'Diario de Noticias'"

Cam Cameron, UM Football, assistant coach, 1989

[from 1989 football media guide]

1985 Quarterbacks, including Jim Harbaugh, UM Football, coaches Cam Cameron and Jerry Hanlon

Back Row: Cam Cameron, Jim Harbaugh, Jim Whitledge, Chris Zurbrugg, Russell Rein, Bob Cernak,

Michael Taylor, Jerry Hanlon, Scott Crawford, Demetrius Brown

1985 Quarterbacks, including Jim Harbaugh, UM Football, coaches Cam Cameron and Jerry Hanlon

Back Row: Cam Cameron, Jim Harbaugh, Jim Whitledge, Chris Zurbrugg, Russell Rein, Bob Cernak,

Michael Taylor, Jerry Hanlon, Scott Crawford, Demetrius Brown

Analysis of O-glycosylation site occupancy in bovine kappa-casein glycoforms separated by two-dimensional gel electrophoresis

The ability of two-dimensional gel electrophoresis (2-DE) to separate glycoproteins was exploited to separate distinct glycoforms of kappa-casein that differed only in the number of O-glycans that were attached. To determine where the glycans were attached, the individual glycoforms were digested in-gel with pepsin and the released glycopeptides were identified from characteristic sugar ions in the tandem mass spectrometry (MS) spectra. The O-glycosylation sites were identified by tandem MS after replacement of the glycans with ammonia/aminoethanethiol. The results showed that glycans were not randomly distributed among the five potential glycosylation sites in kappa-casein. Rather, glycosylation of the monoglycoform could only be detected at a single site, T-152. Similarly the diglycoform appeared to be modified exclusively at T-152 and T-163, while the triglycoform was modified at T-152, T-163 and T-154. While low levels of glycosylation at other sites cannot be excluded the hierarchy of site occupation between glycoforms was clearly evident and argues for an ordered addition of glycans to the protein. Since all five potential O-glycosylation sites can be glycosylated in vivo, it would appear that certain sites remain latent until other sites are occupied. The determination of glycosylation site occupancy in individual glycoforms separated by 2-DE revealed a distinct pattern of in vivo glycosylation that has not been recognized previously.