1. A new method has been developed for the specific extraction of histone fraction f2(a) from calfthymus deoxyribonucleoprotein at pH 7 by using a mixture of ethanol and guanidinium chloride. 2. Fraction f2(a) has been separated into the subfractions f2(a)1 and f2(a)2 by acetone precipitation from acid solution, and at pH7. 3. Modifications of existing electrophoretic methods are described that...

Four unique carboxymethylcysteine-containing peptides were isolated from tryptic and chymotryptic digests of trout muscle actin carboxymethylated with iodo[2-(14)C]acetic acid in 6m-guanidinium chloride. The amino acid sequences of these peptides were determined and showed a high degree of homology with the corresponding sequences from rabbit actin. One of the radioactive peptides was the C-ter...

A guanidinium chloride extract of [3H]glucosamine- and [35S]methionine-labeled virions plus dense bodies of human cytomegalovirus (Towne) was separated by reverse-phase high-pressure liquid chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the eluate revealed the major peak to be a glycoprotein with a relative mass of 64,000. This glycoprotein (HCMVgp64) was character...

IN THE CRYSTAL OF THE TITLE COMPOUND [SYSTEMATIC NAME: 2-(3,5-diamino-6-chloro-pyrazin-2-ylcarbon-yl)guanidinium chloride methanol disolvate], C(6)H(9)ClN(7)O(+)·Cl(-)·2CH(3)OH , the components are connected by N-H⋯N, N-H⋯Cl, N-H⋯O, O-H⋯Cl and O-H⋯O hydrogen bonds into a three-dimensional network. The dihedral angle between the aromatic ring and the guanidine residue is 6.0 (2)°.

The subunit of the Vicia graminea lectin with blood-group-N specificity was examined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and gel filtration in 6M-guanidinium chloride, and its molecular weights was found to be 25 000. The unique N-terminal sequence fof the first nine residues of the lectin confirmed that Vicia lectin consists of four identical chains non-covalently lin...

The title hydrated salt, C7H18N3 (+)·OCN(-).1.5H2O, was synthesized starting from N,N,N',N',N'',N''-hexa-methyl-guanidinium chloride by a twofold anion-exchange reaction. The asymmetric unit contains two cations, two cyanate anions and three water mol-ecules. One cation shows orientational disorder and two sets of N-atom positions were found related by a 60° rotation, with an occupancy ratio of...

Native structures of wild-type proteins may unfold as external conditions change. Usually unfolding occurs as a result of raising temperature, increasing the concentration of denaturants such as urea or guanidinium chloride, or changing pH. Only recently it has been recognized that certain wild-type proteins are subject to external force and in the course of performing biological functions they...

Virus inactivation by a number of protein denaturants commonly used in gel affinity chromatography for protein elution and gel recycling has been investigated. The enveloped viruses Sindbis, herpes simplex-1 and vaccinia, and the non-enveloped virus polio-1 were effectively inactivated by 0.5 M sodium hydroxide, 6 M guanidinium thiocyanate, 8 M urea and 70% ethanol. However, pH 2.6, 3 M sodium ...