O-甲基异脲硫酸盐
O-甲基异脲硫酸盐结构式
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常用名 | O-甲基异脲硫酸盐 | 英文名 | O-Methylisourea hemisulfate |
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| CAS号 | 52328-05-9 | 分子量 | 246.242 | |
| 密度 | N/A | 沸点 | 66.9ºC at 760 mmHg | |
| 分子式 | C4H14N4O6S | 熔点 | 163-167 °C(lit.) | |
| MSDS | 中文版 美版 | 闪点 | 165.7ºC |
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Relative quantification of tau-related peptides using guanidino-labeling derivatization (GLaD) with online-LC on a hybrid ion trap (IT) time-of-flight (ToF) mass spectrometer.
J. Am. Soc. Mass Spectrom. 18(2) , 201-7, (2007) Development of a quantification method based on isotopic variants of O-methyl isourea (OMIU) in conjunction with reversed-phase (RP) liquid chromatography (LC) electrospray mass spectrometry is described for determining the relative quantification of tau-rela... |
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Chemical modification of bovine pancreatic trypsin inhibitor for single site coupling of immunogenic peptides for NMR conformational analysis.
J. Biol. Chem. 264(14) , 7882-8, (1989) Procedures for chemical modification of bovine pancreatic trypsin inhibitor (BPTI) to allow site-specific coupling of immunogenic peptides are reported. Each of the modified proteins has a single free amino group; the other amino groups of lysine or the amino... |
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Chemical modulation of the chaperone function of human alphaA-crystallin.
J. Biochem. 144(1) , 21-32, (2008) alphaA-crystallin is abundant in the lens of the eye and acts as a molecular chaperone by preventing aggregation of denaturing proteins. We previously found that chemical modification of the guanidino group of selected arginine residues by a metabolic alpha-d... |
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Complex formation of guanidinated bovine trypsin inhibitor (Kunitz) with trypsin, chymotrypsin and trypsinogen as studied by the spin-label technique.
FEBS Lett. 140(1) , 53-7, (1982)
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Effect of lysine modification on the conformation and indomethacin binding properties of human serum albumin.
Int. J. Biol. Macromol. 26(2-3) , 173-80, (1999) In order to study the involvement of lysine residues of human serum albumin (HSA) in the binding of indomethacin, HSA was treated with different molar excess of acetic anhydride, succinic anhydride and O-methylisourea which resulted in differently modified pr... |
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Structure-toxicity relationships of neurotoxin RTX-III from the sea anemone Radianthus macrodactylus: modification of amino groups.
Toxicon 29(7) , 819-26, (1991) The effect of modification of amino groups on RTX-III induced lethality in mice has been studied. The toxicity was not affected by guanidination of one or two lysine residues with O-methylisourea, but guanidination of three or four lysine residues decreased l... |
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Involvement of lysine residues in the binding of ovine chorionic somatomammotropin to lactogenic and somatotropic receptors.
FEBS Lett. 166(2) , 352-6, (1984) The biological activities of several ovine chorionic somatomammotropin (oCS) derivatives obtained by chemical modification of the lysine residues were studied by radioreceptor assays using rabbit mammary homogenates (lactogenic activity, L.A.) and liver homog... |
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The antigenic structure of HBsAg: study of the d/y subtype determinant by chemical modification and site directed mutagenesis.
Mol. Immunol. 27(5) , 435-41, (1990) Lysine residue 122 of the major protein of HBsAg/adw has been shown previously to be involved in the d subtype determinant. We demonstrate here that the corresponding residue of the HBsAg/ayw, arginine 122, does not play such a critical role the y site of thi... |
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Arginyl residues and thermal stability in proteins.
Mol. Cell Biochem. 71(2) , 121-7, (1986) Guanidination and amidination of bovine serum albumin, yeast enolase and yeast alcohol dehydrogenase were accompanied by increases in thermal stability at lower extents of modification. Decreases in thermal stability result from greater modification. These re... |
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Kinetics of chemical modification of arginine and lysine residues in calf thymus histone H1.
Biopolymers 20(6) , 1103-12, (1981)
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