Studies in chrome mordanting. II. The binding of chromium(III) cations to wool

1968 ◽  
Vol 21 (11) ◽  
pp. 2723 ◽  
Author(s):  
FR Hartley
Keyword(s):  
Carboxyl Groups ◽  
Thiol Groups ◽  
Amino Groups

The reactions of a number of chromium(111) salts with wool have been investigated. It was found that chromium(111) was not displaced from wool by washing in water. Chromium(111) was bound to wool by the carboxyl groups. Other groups such as sulphonate and thiol groups also bound chromium(111) when these were present, but no evidence was found for binding by amino groups. A mechanism is suggested for the reaction of chromium(111) with wool.

scholarly journals The principle of formaldehyde, alcohol, and acetone titrations. With a discussion of the proof and implication of the zwitterion conception

1934 ◽  
Vol 115 (792) ◽  
pp. 121-141 ◽  
Keyword(s):  
Amino Acids ◽  
Carboxyl Groups ◽  
Recent Discussion ◽  
Amino Groups ◽  
Chemical Methods ◽  
Titration Method ◽  
Physico Chemical ◽  
Empirical Argument ◽  
Chemical Evidence

Consideration of the implications of the zwitterion hypothesis of Bjerrum (1923) makes it desirable to state afresh the principles underlying the methods commonly employed in the titration of amino-acids. Deductions of considerable theoretical importance, cf., e. g ., Calvery (1933) are still being made on the supposition that the alkalimetric formaldehyde titration method of Sørensen (1907) and the corresponding alcohol method of Foreman (1920) and of Willstätter and Waldschmidt-Leitz (1921) estimate the carboxyl groups of amino-acids whilst the acidimetric acetone titration of Linderstrøm-Lang (1928) estimates the amino-groups. Yet the zwitterion hypothesis indicates that this assumption is the reverse of the truth. Discussion is greatly facilitated by collective consideration of recent physico-chemical evidence clarifying the principles upon which these common bio-chemical methods rest. In a recent discussion of two of the titrimetric methods (Van Slyke and Kirk, 1933) the existence of this evidence is ignored, so that it becomes necessary to systematize and elaborate the empirical argument of these authors in the light of the relevant investigations of Grünhut (1919), Cray and Westrip (1925), Michaelis and Mizutani (1925), Birch and Harris (1930, b ), and Levy (1933). At the same time new and useful developments are indicated.

Reaction of Fluorescein Isothiocyanate with Thiol and Amino Groups of Sarcoplasmic ATPase

1985 ◽  
Vol 40 (11-12) ◽  
pp. 863-875 ◽  
Author(s):  
Gertrude Swoboda ◽  
Wilhelm Hasselbach
Keyword(s):  
Absorption Maximum ◽  
Sodium Dodecylsulfate ◽  
Specific Effect ◽  
Fluorescein Isothiocyanate ◽  
Thiol Groups ◽  
Amino Groups ◽  
Model Compounds ◽  
Intramolecular Transfer ◽  
Dodecyl Ether ◽  
Lysyl Residue

Abstract Several model compounds containing thiol and/or amino groups (mercaptoethanol, glutathione, cysteine, ethanolamine, glycine) were studied with respect to their reactivity towards fluorescein isothiocyanate (followed spectrophotometrically at 504 and 412 nm), stability of product and long­ wave absorption maximum of the fluorescein residue attached. Thiol groups reacted by far more readily than amino groups. A specific effect was observed with cysteine, indicating an intramolecular transfer of the fluorescein residue from SH to NH2.With sarcoplasmic vesicles both types of reactions were observed. The ratio of products, which can be distinguished by their different stabilities and absorption spectra, depended on the absence or presence of detergents. While with native vesicles the NH2 reaction predominated, with vesicles solubilized with sodium dodecylsulfate, octaethyleneglycol mono-n-dodecyl ether or 1-0-tetradecyl-propanediol-(1,3)-3-phosphorylcholine the SH reaction became prevailing. Already 0.35 mg sodium dodecylsulfate per mg protein were sufficient to give rise to dithiourethane formation exclusively. Excess fluorescein isothiocyanate reacted with several thiol groups of dodecylsulfate-solubilized vesicles. In the presence of ATP binding of fluorescein isothiocyanate to native vesicles was significantly reduced.Total blockage of the vesicular SH groups with N-ethyl-maleimide led to preparations that reacted with fluorescein isothiocyanate much more slowly, compared to native vesicles. Octaethy­ leneglycol mono-n-dodecyl ether or 1-0-tetradecyl-propanediol-(1,3)-3-phosphorylcholine in the assay accelerated the thioureide formation from N-ethylmaleimide modified vesicles, whereas sodium dodecylsulfate prevented it almost completely.Our results support the suggestion that one or several thiol groups in vicinity of the highly reactive lysyl residue might play a role in the fast specific reaction, which is only observed with intact native vesicles.

Self-assembly of strawberry-like organic–inorganic hybrid particle clusters with directionally distributed bimetal and facile transformation of the core and corona

2020 ◽  
Vol 11 (18) ◽  
pp. 3136-3151 ◽  
Author(s):  
Shuxing Mei ◽  
Mingwang Pan ◽  
Juan Wang ◽  
Xiaopeng Zhang ◽  
Shaofeng Song ◽  
...  
Keyword(s):  
Strong Interaction ◽  
Self Assembly ◽  
Carboxyl Groups ◽  
Amino Groups ◽  
Inorganic Hybrid ◽  
Inorganic Particles ◽  
Hybrid Particle ◽  
The Core ◽  
Organic Particles ◽  
Facile Transformation

Controllable structure of organic–inorganic hybrid particle clusters were successfully fabricated by self-assembly which derived from the strong interaction between carboxyl groups of the organic particles and amino groups of the inorganic particles.

scholarly journals The reaction of aldolase with 2-methylmaleic anhydride

1970 ◽  
Vol 116 (5) ◽  
pp. 843-849 ◽  
Author(s):  
I. Gibbons ◽  
R. N. Perham
Keyword(s):  
Enzyme Activity ◽  
Maleic Anhydride ◽  
Enzymic Activity ◽  
Side Reactions ◽  
Rabbit Muscle ◽  
Thiol Groups ◽  
Amino Groups ◽  
Partial Loss ◽  
Reaction Proceeds ◽  
Citraconic Anhydride

1. The reaction of rabbit muscle aldolase with 2-methylmaleic anhydride is described. All the protein amino groups can be reversibly blocked. 2. As the reaction proceeds, the enzyme activity decreases until, at about 50% citraconylation of amino groups, the enzyme is completely inhibited. At this stage, little or no dissociation of the enzyme tetramer is observed and 75% of the activity is recoverable on unblocking the amino groups. 3. At 80% blocking, the enzyme is completely dissociated but little enzymic activity is recoverable after unblocking. Inability to recover activity after citraconylation and unblocking correlates with the onset of dissociation of the citraconyl-aldolase seen on ultracentrifugation. 4. The only irreversible modification of the enzyme primary structure detectable after the citraconylation and unblocking reactions is the partial loss of thiol groups. It is probable that this is responsible for the inability to reform active enzyme from the citraconylated subunit. 5. Other reversible side reactions of maleic anhydride and citraconic anhydride that may occur with proteins are discussed.

Highly selective and sensitive biosensing of dopamine based on glutathione coated silver nanoclusters enhanced fluorescence

2017 ◽  
Vol 41 (24) ◽  
pp. 15244-15250 ◽  
Author(s):  
Ramar Rajamanikandan ◽  
Malaichamy Ilanchelian
Keyword(s):  
Hydrogen Bonding ◽  
Emission Intensity ◽  
Silver Nanoclusters ◽  
Carboxyl Groups ◽  
Hydrogen Bonding Interaction ◽  
Amino Groups ◽  
Enhanced Fluorescence ◽  
Bonding Interaction

The emission intensity of red emissive GSH-AgNCs is notably enhanced after the addition of dopamine. The increasing emission intensity is attributed to the hydrogen bonding interaction between the carboxyl groups of GSH-AgNCs and amino groups of dopamine.

scholarly journals Positive Charges on Lysine Residues of the Extrinsic 18 kDa Protein Are Important to Its Electrostatic Interaction with Spinach Photosystem II Membranes

2005 ◽  
Vol 37 (11) ◽  
pp. 737-742 ◽  
Author(s):  
Jin-Peng Gao ◽  
Zhen-Hua Yong ◽  
Feng Zhang ◽  
Kang-Cheng Ruan ◽  
Chun-He Xu ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Methyl Esters ◽  
Binding Activity ◽  
Water Soluble ◽  
Carboxyl Groups ◽  
Amino Groups ◽  
Charged Amino Acids ◽  
Lysine Residues ◽  
Glycine Methyl Ester ◽  
Positively Charged

Abstract To determine the contribution of charged amino acids to binding with the photosystem II complex (PSII), the amino or carboxyl groups of the extrinsic 18 kDa protein were modified with Nsuccinimidyl propionate (NSP) or glycine methyl ester (GME) in the presence of a water-soluble carbodiimide, respectively. Based on isoelectric point shift, 4–10 and 10–14 amino groups were modified in the presence of 2 and 4 mM NSP, respectively. Similarly, 3–4 carboxyl groups were modified by reaction with 100 mM GME. Neutralization of negatively charged carboxyl groups with GME did not alter the binding activity of the extrinsic 18 kDa protein. However, the NSP-modified 18 kDa protein, in which the positively charged amino groups had been modified to uncharged methyl esters, failed to bind with the PSII membrane in the presence of the extrinsic 23 kDa protein. This defect can not be attributed to structural or conformational alterations imposed by chemical modification, as the fluorescence and circular dichroism spectra among native, GME and NSP-modified extrinsic 18 kDa proteins were similar. Thus, we have concluded that the positive charges of lysyl residues in the extrinsic 18 kDa protein are important for its interaction with PSII membranes in the presence of the extrinsic 23 kDa protein. Furthermore, it was found that the negative charges of carboxyl groups of this protein did not participate in binding with the extrinsic 23 kDa protein associated with PSII membranes.

scholarly journals REACTION OF ENZYMES AND PROTEINS WITH MUSTARD GAS (BIS(ß-CHLOROETHYL)SULFIDE)

1946 ◽  
Vol 30 (2) ◽  
pp. 185-210 ◽  
Author(s):  
Roger M. Herriott ◽  
M. L. Anson ◽  
John H. Northrop
Keyword(s):  
Qualitative Difference ◽  
Reaction Rates ◽  
Carboxyl Groups ◽  
Mustard Gas ◽  
Amino Groups ◽  
Rate Of Reaction ◽  
Extreme Variation ◽  
H Protein ◽  
Phenol Reagent ◽  
Yeast Hexokinase

1. The rate of reaction of mustard gas (H) with thirteen proteins has been determined. The extreme variation in reaction rates is about 100:1. 2. No qualitative difference in the results was observed when the treatment with H was carried out by the Dixon or stirring methods. 3. The kinetics have been analyzed and a bimolecular equation derived which fits the facts. 4. The carboxyl groups of all proteins reacted when the reaction with H was carried out at pH 6.0 in M/25 acetate buffer. In most cases the number of carboxyl groups covered was approximately equal to the number of H residues bound. 5. The amino groups of proteins failed to react with the possible exception of yeast hexokinase. 6. The color obtained when proteins were mixed with Folin's phenol reagent at pH 8.0 decreased as the protein was treated with H. The color returned on treatment of the H-protein with alkali and many of the combined H groups were hydrolyzed. Similar results were observed when a concentrated glycyltyrosine solution was treated with H.

scholarly journals Effect of Pentacyclic Guanidine Alkaloids from the Sponge Monanchora pulchra on Activity of α-Glycosidases from Marine Bacteria

Marine Drugs ◽  
2019 ◽  
Vol 17 (1) ◽  
pp. 22 ◽  
Author(s):  
Irina Bakunina ◽  
Galina Likhatskaya ◽  
Lubov Slepchenko ◽  
Larissa Balabanova ◽  
Liudmila Tekutyeva ◽  
...  
Keyword(s):  
Marine Bacteria ◽  
Active Site ◽  
Binding Sites ◽  
Marine Bacterium ◽  
Competitive Inhibitor ◽  
Carboxyl Groups ◽  
Northwest Pacific ◽  
Amino Groups ◽  
Irreversible Inhibitors ◽  
Guanidine Alkaloids

The effect of monanchomycalin B, monanhocicidin A, and normonanhocidin A isolated from the Northwest Pacific sample of the sponge Monanchora pulchra was investigated on the activity of α-galactosidase from the marine γ-proteobacterium Pseudoalteromonas sp. KMM 701 (α-PsGal), and α-N-acetylgalactosaminidase from the marine bacterium Arenibacter latericius KMM 426T (α-NaGa). All compounds are slow-binding irreversible inhibitors of α-PsGal, but have no effect on α-NaGa. A competitive inhibitor d-galactose protects α-PsGal against the inactivation. The inactivation rate (kinact) and equilibrium inhibition (Ki) constants of monanchomycalin B, monanchocidin A, and normonanchocidin A were 0.166 ± 0.029 min−1 and 7.70 ± 0.62 μM, 0.08 ± 0.003 min−1 and 15.08 ± 1.60 μM, 0.026 ± 0.000 min−1, and 4.15 ± 0.01 μM, respectively. The 2D-diagrams of α-PsGal complexes with the guanidine alkaloids were constructed with “vessel” and “anchor” parts of the compounds. Two alkaloid binding sites on the molecule of α-PsGal are shown. Carboxyl groups of the catalytic residues Asp451 and Asp516 of the α-PsGal active site interact with amino groups of “anchor” parts of the guanidine alkaloid molecules.

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