Guanidinium sulphate

Kon kova TS, Matyushin YuN, Miroshnichenko EA, Vorob ev AB (2009) Thermochemical properties of dinitramidic acid salts. Russ Chem Bull Inti Ed 58 2020-2027 Kumar A (2001a) Aqueous guanidinium salts Part ll. Isopiestic osmotic coefficients of guanidinium sulphate and viscosity and surface tension of guanidinium chloride, bromide, acetate, perchlorate and sulphate solutions at 298.15 K. Eluid Phase Equil 180 195-204 Kumar A (2001b) Aqueous guanidinium salts part I. Densities, ultrasonic velocities, and apparent molar properties. J Solution Chem 30 281-290... 

Electronic Raman Spectrum of Guanidinium Vanadium Sulphate... 

Cr4(OH)6(en)6] , as its sulphate and azide salts, have been published. The alkali-metal and guanidinium salts of the heteropoly-anion [CrZnWii04oH2] have been isolated following substitution of Cr for the octahedrally co-ordinated Zn in [Zn2Wn04oH2] . ... 

Chondroitin sulphate proteoglycan, devoid of any affinity to hyaluronic acid, and dermatan sulphate proteoglycan have been isolated after extraction of proteoglycans from pig skin with guanidinium chloride at low temperatures and in the presence of protease inhibitors. Some chemical and physical properties of the products were reported. However, a chondroitin sulphate proteoglycan from cultured human glial cells has been shown to bind to hyaluronic acid. ... 

The effects of dimethyl sulphoxide, lithium bromide, guanidinium chloride, sodium dodecyl sulphate, and urea on lysozyme have been studied using Raman spectroscopy. The spectrum observed was found to depend on the denaturant used, suggesting there is not a unique denatured state for lysozyme. An analysis of the interaction of sodium dodecyl sulphate with lysozyme has been published. A kinetic study of the denaturation and subsequent reduction of disulphide bonds in lysozyme has been made using rapid ultrasonic absorption measurements. 

X 10 ) in the presence of sodium dodecyl sulphate or guanidinium hydrochloride, contains pyridoxal phosphate, and is stable in the pH-range... 

The properties of a-D-galactosidase (mol. wt. 3.0 x 10 ) from Saccharomyces carlsbergensis have been shown to be similar to those of other extracellular enzymes in yeast. The carbohydrate content (57 %) consists of D-mannose (ca. 92%), D-glucose (7%), and 2-amino-2-deoxy-D-glucose (1%) 35% of its amino acid residues can be accounted for by L-threonine, L-serine, and l-aspartic acid. Although the enzyme remains active after treatment with sodium dodecyl sulphate, it is denatured by urea and guanidinium chloride. With urea or 60 °C heat denaturation, the enzyme dissociates into two types of subunits and was therefore considered to be the first reported external enzyme from yeast with an oligomeric structure. 

The effect of hydration on the thermal denaturation of lysozyme as measured by differential scanning calorimetry has been examined. Tht Raman spectrum of chemically denatured (dimethyl sulphoxide, urea, LiBr, guanidinium chloride, sodium dodecyl sulphate) hen egg-white lysozyme has been studied. ... 

A homogeneous preparation of reduced and carboxymethylated )3-ovomucin has been shown to contain a subunit of molecular weight 1.12 x 10 , sulphate (4.24%), and carbohydrate (60%) consisting largely of D-galactose (22%), 2-amino-2-deoxy-D-galactose (8.9%), and sialic acid (10.6%). A soluble, fibrous component extracted from crude ovomucin with SM-guanidinium chloride contained 70% jS-ovomucin. 

The isoenzymes of rat-liver microsomal /S-D-glucuronidase showed different responses to such dissociating agents as urea, guanidinium hydrochloride, and sodium dodecyl sulphate. Loss of catalytic activity in the denaturing media is accompanied by dissociation of the enzymes into subunits. Gel electrophoresis in the presence of sodium dodecyl sulphate revealed that the enzymes are tetramers consisting of different proportions of three types of glycoprotein subunit (mol. wts. 6.29 X 10 , 6.02 X 10 , and 5.87 x 10 ). 

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