Disease relevance of guanidine

• Nucleic acids were extracted from serum, saliva, and semen in guanidinium thiocyanate, subjected to reverse transcription, and then amplified by a double polymerase chain reaction technique using "nested" primers from the highly conserved 5' non-coding region of the hepatitis C virus genome [1].
• We have produced via site-directed mutagenesis two Escherichia coli alkaline phosphatase mutants (lysine-166 and glutamine-166) to test whether the guanidinium group plays a critical role in catalysis [2].
• In addition to the inactivation by thiocyanate ions, other chaotropic ions such as guanidinium and trichloroacetate inactivate the scrapie agent [3].
• HOL1 double mutants and, to a lesser extent, HOL1-1 single mutants show hypersensitivity to specific cations added to the growth medium, including Na+, Li+, Cs+, Be2+, guanidinium ion, and histidinol, but not K+, Rb+, Ca2+, or Mg2+ [4].
• Residual guanidinium depressed the rate of Rhodospirillum rubrum ribulose-1,5-bisphosphate carboxylase (Rubisco) folding; an increased aggregation rate also decreased the yield of folded Rubisco [5].

Psychiatry related information on guanidine

• Total cellular polyadenylated RNA (poly(A)+ RNA, mRNA) was prepared after guanidinium thiocyanate extraction of frozen brain tissue from age-matched controls and patients suffering from schizophrenia and unipolar depression [6].

High impact information on guanidine

• The deduced molecular weight agrees with gel filtration results provided the more chaotropic denaturant 6 M guanidinium thiocyanate is substituted for the weaker guanidinium chloride [7].
• Inhibitors combining guanidinium-like structural motifs with long chains specifically targeting this residue are good candidates for rational isoform-specific drug design [8].
• In particular, the structure of pSRII exhibits a largely unbent conformation of the retinal (as compared with bacteriorhodopsin and halorhodopsin), a hydroxyl group of Thr-204 in the vicinity of the Schiff base, and an outward orientation of the guanidinium group of Arg-72 [9].
• We have recently discovered that cationic cholesterol derivatives characterized by guanidinium polar headgroups are very efficient for gene transfection in vitro and in vivo [10].
• Synthesis, biophysical properties, and nuclease resistance properties of mixed backbone oligodeoxynucleotides containing cationic internucleoside guanidinium linkages: deoxynucleic guanidine/DNA chimeras [11].

Chemical compound and disease context of guanidine

• The molecular weights of the three nonidentical subunits of citrate lyase of Klebsiella aerogenes have been determined by three methods: sedimentation equilibrium in 6 M guanidinium chloride, sodium dodecyl sulfate gel electrophoresis, and gel filtration on 6 percent agarose column in 6 M guanidinium chloride [12].
• The maganese-containing superoxide dismutase, from Escherichia coli, lost metal and activity when dialyzed against 20 mM-8-hydroxyquinoline and 2.5 M guanidinium chloride in 5 mM Tris-chloride buffer at pH 7 [13].
• A partially unfolded state of the Fe4S4-containing high potential iron-sulfur protein from Chromatium vinosum has been detected and characterized by NMR spectroscopy following addition of a concentrated solution of guanidinium chloride to the native protein [14].
• NC10 scFv was purified by solubilization of the E. coli membrane fraction with guanidinium hydrochloride followed by column chromatography [15].
• A range of DNA isolation strategies was developed for isolating M. avium subsp. paratuberculosis DNA from spiked milk, the most effective of which involved the use of 50 mM Tris HCl, 10 mM EDTA, 2% Triton X-100, 4 M guanidinium isothiocyante, and 0.3 M sodium acetate combined with boiling, physical grinding, and nucleic acid spin columns [16].

Biological context of guanidine

• Thus, the stabilizing effect of the positively charged guanidinium group does not appear to play a major role in the rate-limiting step for substrate hydrolysis [2].
• The guanidinium group of arginine-166 has been postulated to act as an electrophilic species during phosphorylation of alkaline phosphatase [2].
• These findings indicate that mu-conotoxins must be classified in the same group of Na channel inhibitors as guanidinium toxins, since they competed with guanidinium toxins for binding sites on the Na channel [17].
• Mu-Conotoxins (CGIIIA and CGIIIB) and guanidinium toxins (TTX and saxitoxin) inhibited 3H-Pr-CGIIIA (1 nM) binding to electroplax membranes with IC50 values of 0.6, 1.1, 7.1, and 2.2 nM, respectively [17].
• One type which is resistant to 5.2 M guanidinium chloride is most likely a D-loop that depends only on heteroduplex base pairing for its stability [18].

Anatomical context of guanidine

• Structure/activity studies based on transport measurements in vesicles prepared from guinea pig left ventricle indicate that hydrophobic substitutions at the terminal nitrogen atom of the guanidinium moiety of amiloride improved the inhibitory potency almost 100-fold over that of the parent compound [19].
• Treatment of macaques with 2 mg/kg of the guanidinium compounds resulted in patches of small-cell infiltrate, slight neuronal loss, and degenerative alterations in the sympathetic ganglia [20].
• Low density proteoglycans (PG-III) were isolated from bovine articular cartilage by extraction with 4 M guanidinium chloride followed by sedimentation in a dissociative CsCl density gradient and fractionation by chromatography on DEAE-cellulose and Sepharose CL-6B columns [21].
• Based on these results, we propose that the guanidinium group binds to a relatively wide vestibule at the cytoplasmic surface; but, unlike Na+ or K+ ions, it cannot pass into a narrower region of the cation transport path within the membrane [22].
• Static and dynamic light-scattering methods have been used to investigate the structure of chick limb bud chondrocyte proteoglycan aggregate in 0.4 M guanidinium chloride [23].

Associations of guanidine with other chemical compounds

• Nucleolar antigen p145 was released from ribonucleoproteins following treatment with 4 M guanidinium hydrochloride or RNase [24].
• We find that the non-reactive guanidinium nitrogen of L-arginine binds in a pocket that is relatively intolerant of changes in the size or hydrogen bonding properties of the group bound [25].
• The guanidinium chloride-mediated denaturation of KBPAP was monitored by several structural and functional parameters viz. activity, tryptophan fluorescence, 8-anilinonaphthalene 1-sulfonic acid binding, circular dichroism, and size exclusion chromatography, in the presence and absence of 10 mm phosphate [26].
• On denaturation, the enzyme dissociated into two similar, if not identical, subunits which possessed a molecular weight of 34,000 by sodium dodecyl sulfate/urea-polyacrylamide gel electrophoresis and a weight average molecular weight of 35,000 by sedimentation equilibrium in the presence of 4.0 M guanidinium chloride [27].
• Thus, the hydrophobic side chains of leucine-73 and leucine-75 and the guanidinium group of arginine-77 are important for the contractile activity of the active site COOH-terminal pentapeptide of human C3a anaphylatoxin [28].

Gene context of guanidine

• Imidazoline/guanidinium binding domains on monoamine oxidases. Relationship to subtypes of imidazoline-binding proteins and tissue-specific interaction of imidazoline ligands with monoamine oxidase B [29].
• However, [KIL-d] is distinct from the known yeast prions in its relative guanidinium hydrochloride incurability and independence of Hsp104 protein for its maintenance [30].
• Human gastric mucin was isolated by successive CsCl-gradient ultracentrifugation in the presence of guanidinium hydrochloride to prevent degradation of the polypeptide moieties of the molecules [31].
• Extraction of the recombinant proteins from inclusion bodies by guanidinium chloride, followed by two column chromatography steps, produced high yields of pure CNTF that supported survival and neurite outgrowth from embryonic chick ciliary neurons in culture [32].
• In HSMSL saliva, MUC5B was found in the gel phase; however, most of the material was 'insoluble' in guanidinium chloride and was only brought into solution by reduction [33].

Analytical, diagnostic and therapeutic context of guanidine

• Their guanidinium chloride unfolding has been studied by circular dichroism spectroscopy [34].
• Two proteins of Mr = 58,000 and 59,000, respectively, were purified from 4 M guanidinium chloride extracts of articular cartilage by dissociative CsCl-density gradient centrifugation followed by gel chromatography on Sephadex G-200 and ion exchange chromatography on DEAE-cellulose [35].
• The thermotropic polymorphism of a series of guanidinium alkanesulfonates (6 < or = n < or = 18) was investigated by optical microscopy and differential scanning calorimetry [36].
• Rather than behaving as a homogenous ensemble of random coils, chemical shift changes for the majority of backbone amide resonances indicate that the denatured ensemble undergoes two definable equilibrium transitions upon titration with guanidinium, in addition to the major refolding event [37].
• This RCA fraction was further resolved into three calmodulin antagonist polypeptides (RCA1, RCA2, and RCA3) by denaturation in the presence of guanidinium HCl and mercaptoethanol and subsequent reverse-phase HPLC on a C8 column eluted with an acetonitrile gradient in the presence of 0.1% trifluoroacetic acid [38].

References