muramidase and methylmercuric-chloride

muramidase has been researched along with methylmercuric-chloride* in 1 studies

Other Studies

1 other study(ies) available for muramidase and methylmercuric-chloride

Article	Year
Counting sulfhydryls and disulfide bonds in peptides and proteins using mercurial ions as an MS-tag. Journal of the American Society for Mass Spectrometry, 2008, Volume: 19, Issue:8 Organic mercurial compounds are the most specific and sensitive reagents for reaction with the sulfhydryl groups (SHs) in peptides and proteins because of the strong mercury-sulfur affinity. Using the monofunctional organic mercury ion RHg(+) as a mass spectrometry (MS)-tag has the advantages of reacting with one sulfhydryl group, offering definite mass shift, and especially stable and characteristic nonradioactive isotopic distribution. Mass spectrometric analysis of derivatized sulfhydryls in peptides/proteins is thus an alternative for precisely counting the number of sulfhydryl groups and disulfide bonds (SS). Here the tags used include monomethylmercury chloride, monoethylmercury chloride, and 4-(hydroxymercuri) benzoic acid. The feasibility of this strategy is demonstrated using HPLC/ESI-MS to count SHs and SS in model peptides/proteins, i.e., glutathione, phytochelatins, lysozyme and beta-lactoglobulin, which contain increasing SHs and various SS linkages. Topics: Chromatography, High Pressure Liquid; Disulfides; Ethylmercuric Chloride; Glutathione; Indicators and Reagents; Mercury; Methylmercury Compounds; Muramidase; Peptides; Proteins; Spectrometry, Mass, Electrospray Ionization; Sulfhydryl Compounds	2008

Article

Year

Counting sulfhydryls and disulfide bonds in peptides and proteins using mercurial ions as an MS-tag.

Journal of the American Society for Mass Spectrometry, 2008, Volume: 19, Issue:8

Organic mercurial compounds are the most specific and sensitive reagents for reaction with the sulfhydryl groups (SHs) in peptides and proteins because of the strong mercury-sulfur affinity. Using the monofunctional organic mercury ion RHg(+) as a mass spectrometry (MS)-tag has the advantages of reacting with one sulfhydryl group, offering definite mass shift, and especially stable and characteristic nonradioactive isotopic distribution. Mass spectrometric analysis of derivatized sulfhydryls in peptides/proteins is thus an alternative for precisely counting the number of sulfhydryl groups and disulfide bonds (SS). Here the tags used include monomethylmercury chloride, monoethylmercury chloride, and 4-(hydroxymercuri) benzoic acid. The feasibility of this strategy is demonstrated using HPLC/ESI-MS to count SHs and SS in model peptides/proteins, i.e., glutathione, phytochelatins, lysozyme and beta-lactoglobulin, which contain increasing SHs and various SS linkages.

Topics: Chromatography, High Pressure Liquid; Disulfides; Ethylmercuric Chloride; Glutathione; Indicators and Reagents; Mercury; Methylmercury Compounds; Muramidase; Peptides; Proteins; Spectrometry, Mass, Electrospray Ionization; Sulfhydryl Compounds

2008