scholarly journals On the disulphide bonds of rhodopsins

1987 ◽  
Vol 246 (1) ◽  
pp. 131-137 ◽  
Author(s):  
S Al-Saleh ◽  
M Gore ◽  
M Akhtar
Keyword(s):  
Acetic Acid ◽  
Indirect Evidence ◽  
Iodoacetic Acid ◽  
The Other ◽  
Cysteine Residues ◽  
Disulphide Bridge ◽  
Disulphide Bonds ◽  
Peptide Purification ◽  
Reducing Conditions ◽  
Bovine Rhodopsin

Carboxymethylation using 14C- or 3H-labelled iodoacetic acid has been used to identify the cysteine residues in bovine rhodopsin involved in the formation of the two intramolecular disulphide bridges. Iodo[2-14C]acetic acid was used to modify 5.8-5.9 residues of cysteine under non-reducing conditions. After dialysis and reduction of disulphide bridges by 2-mercaptoethanol, iodo[2-3H]acetic acid was employed to covalently modify 3.3-3.6 residues of cysteine. Peptide purification and sequencing has unambiguously shown that cysteine residues 322 and 323 are only carboxymethylated after reduction of disulphide bridges. Indirect evidence presented, now coupled with the earlier finding [Findlay & Pappin (1986) Biochem. J. 238, 625-642] suggests that the other disulphide bridge is formed between cysteine residues 110 and 187. A comparison is made of all the sequences of mammalian rhodopsins and colour pigments and attention is drawn to the fact that whereas Cys-322 and Cys-323 are conserved only in three rhodopsins (bovine, ovine and human), the residues corresponding to Cys-110 and Cys-187 are found in all the visual proteins (from rods as well as human cones).

scholarly journals Assignment of a single disulphide bridge in human α2-antiplasmin: implications for the structural and functional properties

1997 ◽  
Vol 323 (3) ◽  
pp. 847-852 ◽  
Author(s):  
Søren CHRISTENSEN ◽  
Zuzana VALNICKOVA ◽  
Ida B. THØGERSEN ◽  
Eva H. N. OLSEN ◽  
Jan J. ENGHILD
Keyword(s):  
Functional Analysis ◽  
Acetic Acid ◽  
Blood Coagulation ◽  
Proteinase Inhibitors ◽  
Serine Proteinase ◽  
Thiol Groups ◽  
Disulphide Bridge ◽  
Disulphide Bonds ◽  
Functional Aspects ◽  
Structural And Functional Properties

Human α2-antiplasmin (α2AP) is a serpin involved in the regulation of blood coagulation. Most serpins, unlike smaller serine proteinase inhibitors, do not contain disulphide bridges. α2AP is an exception from this generalization and has previously been shown to contain four Cys residues organized into two disulphide bridges [Lijnen, Holmes, van Hoef, Wiman, Rodriguez and Collen (1987) Eur. J. Biochem. 166, 565–574]. However, we found that α2AP incorporates iodo[14C]acetic acid, suggesting that the protein contains reactive thiol groups. This observation prompted a re-examination of the state of the thiol groups, which revealed (i) a disulphide bridge between Cys43 and Cys116, (ii) that Cys76 is bound to a cysteinyl-glycine dipeptide, and (iii) and Cys125 exists as either a free thiol or in a mixed disulphide with another Cys residue. The disulphide identified between Cys43 and Cys116 appears to be conserved in orthologous proteins since the homologous Cys residues form disulphide bonds in bovine and possibly mouse α2AP. The conservation of this disulphide bridge suggests that it is important for functional aspects of α2AP. However, the structural and functional analysis described in this study does not support this conclusion.

scholarly journals The accessibility of the thiol groups on G- and F-actin of rabbit muscle

1990 ◽  
Vol 266 (2) ◽  
pp. 453-459 ◽  
Author(s):  
D F Liu ◽  
D Wang ◽  
A Stracher
Keyword(s):  
Thiol Group ◽  
Iodoacetic Acid ◽  
Drastic Change ◽  
The Other ◽  
Cysteine Residues ◽  
Rabbit Muscle ◽  
Thiol Groups ◽  
Filamentous Actin ◽  
Other Hand

The accessibility of the cysteine residues of actin from rabbit muscles to the thiol-targeted reagent 7-dimethylamino-4-methyl-(N-maleimidyl)coumarin (DACM) was investigated. Under conditions where the actin is in the unpolymerized form (G-actin), the most reactive thiol group was Cys-257, suggesting that it was located on the surface of the actin molecule. The selective modification of Cys-374 for this reagent as reported by Sutoh [(1982) Biochemistry 21, 3654-3661] was not observed. Cys-10, Cys-217 and Cys-374 were much less reactive and only gradually became extensively modified when the concentration of DACM approached 5 molar equivalents of actin. Presumably these thiol groups were located further inward away from the surface or situated in a different environment that rendered them less reactive. On the other hand, Cys-285 was completely inaccessible and presumably was buried. The lack of preferential labelling of Cys-374 by DACM is incompatible with the finding with iodoacetic acid as the reagent as reported by Elzinga & Collins [(1975) J. Biol. Chem. 250, 5897-5905]. This discrepancy, however, might well be due to the different reagents employed. The DACM-G-actin largely retained its competence for polymerization. Upon polymerization of G-actin, practically all the thiol groups became inaccessible to DACM, suggesting that a drastic change occurred in the conformation of actin units in the transition of monomers to filamentous actin.

Identification of novel α-gliadin genes

Genome ◽  
2011 ◽  
Vol 54 (3) ◽  
pp. 244-252 ◽  
Author(s):  
Peng-Fei Qi ◽  
Yu-Ming Wei ◽  
Qing Chen ◽  
Thérèse Ouellet ◽  
Jia Ai ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Triticum Aestivum L ◽  
Protein Band ◽  
Cysteine Residues ◽  
Disulphide Bonds ◽  
Chain Extenders ◽  
Domain I ◽  
Unique Domain

Ten novel α-gliadin genes (Gli-ta, Gli-turg1, Gli-turg2, Gli-turg3, Gli-turg4, Gli-turg5, Gli-turg6, Gli-cs1, Gli-cs2, and Gli-cs3) with unique characteristics were isolated from wheat ( Triticum aestivum L.), among which Gli-cs1, Gli-cs2, Gli-cs3, and Gli-turg6 were pseudogenes. Gli-cs3 and nine other sequences were much larger and smaller, respectively, than the typical α-gliadins. This variation was caused by insertion or deletion of the unique domain I and a polyglutamine region, possibly the result of illegitimate recombination. Consequently, Gli-cs3 contained 10 cysteine residues, whereas there were 2 cysteine residues only in the other nine sequences. Gli-ta/Gli-ta-like α-gliadin genes are normally expressed during the development of seeds. SDS–PAGE analysis showed that in-vitro-expressed Gli-ta could form intermolecular disulphide bonds and could be chain extenders. A protein band similar in size to Gli-ta has been observed in seed extracts, and mass spectrometry results confirm that the band contains small molecular mass α-gliadins, which is a characteristic of the novel α-gliadins. Mass spectrometry results also indicated that the two cysteine residues of Gli-ta/Gli-ta-like proteins participated in the formation of intermolecular disulphide bonds in vivo.

scholarly journals Synthesis of spiro[dihydropyridine-oxindoles] via three-component reaction of arylamine, isatin and cyclopentane-1,3-dione

2013 ◽  
Vol 9 ◽  
pp. 8-14 ◽  
Author(s):  
Yan Sun ◽  
Jing Sun ◽  
Chao-Guo Yan
Keyword(s):  
Acetic Acid ◽  
Reaction Mechanism ◽  
Room Temperature ◽  
The Other ◽  
Other Hand ◽  
Three Component Reaction ◽  
High Yields

A fast and convenient protocol for the synthesis of novel spiro[dihydropyridine-oxindole] derivatives in satisfactory yields was developed by the three-component reactions of arylamine, isatin and cyclopentane-1,3-dione in acetic acid at room temperature. On the other hand the condensation of isatin with two equivalents of cyclopentane-1,3-dione gave 3,3-bis(2-hydroxy-5-oxo-cyclopent-1-enyl)oxindole in high yields. The reaction mechanism and substrate scope of this novel reaction is briefly discussed.

Preparations, sulphinate coordination, and thermal decomposition of some bismuth triarenesulphinates

1972 ◽  
Vol 25 (10) ◽  
pp. 2107 ◽  
Author(s):  
GB Deacon ◽  
GD Fallon
Keyword(s):  
Thermal Decomposition ◽  
Acetic Acid ◽  
Sulphur Dioxide ◽  
Glacial Acetic Acid ◽  
The Other

Bismuth triarenesulphinates, Bi(02SR)3 [R = Ph, p-MeC6H4, p-ClC6H4, 2,4,6-(Me2CH)3C6H2, and p-MeCONHC6H4], have been prepared by reaction of bismuth triacetate with the appropriate arenesulphinio acids in glacial acetic acid, and the first two compounds have also been obtained by reaction of triphenyl-bismuth with the appropriate mercuric arenesulphinates. The sulphur-oxygen stretching frequencies of the bismuth sulphinates are indicative of O-sulphinate coordination, and the compounds are considered to be polymeric with bridging O-sulphinate groups and six-coordinate bismuth. Thermal decomposition of Bi(O2SR)3 (R = Ph, p-MeC6H4, or p-CIC6H4) under vacuum gave the corresponding triarylbismuth compounds and sulphur dioxide, the preparation of tri-p-chlorophenylbismuth being accompanied by formation of di-p-chlorophenyl sulphone and S-p-chlorophenyl p-chlorobenzenethiosulphonate. Pyrolysis of the other triarenesulphinates did not yield organobismuth compounds.

Changes in protein spectra of bean seed during germination

1970 ◽  
Vol 48 (7) ◽  
pp. 1347-1350 ◽  
Author(s):  
Pei-Show Juo ◽  
G. Stotzky
Keyword(s):  
Acetic Acid ◽  
Phaseolus Vulgaris ◽  
Basic Protein ◽  
The Other ◽  
Globulin Fraction ◽  
Bean Seed ◽  
Basic Proteins ◽  
Number Of Components ◽  
Red Kidney Bean ◽  
Protein Spectra

Globulins, albumins, and basic proteins were extracted from seeds of red kidney bean (Phaseolus vulgaris), and their distribution was in a ratio of about 3:2:1, respectively. The globulin fraction constituted a major portion of the reserve proteins and was hydrolyzed rapidly during germination. More than 90% of the basic proteins, extractable with 0.05 N acetic acid, disappeared 12 days after germination. Although the decrease in total albumin was not as marked as with the other two fractions, a number of components of this fraction disappeared during the early stages of germination, but several new components were detected about 8 days after germination. The apparent synthesis of new globulin components during germination was also observed, but no synthesis of basic protein could be detected.

Cell adhesion and phagocytosis promoted by monoclonal antibodies not directed against fibronectin receptors

1988 ◽  
Vol 90 (2) ◽  
pp. 201-214 ◽  
Author(s):  
F. Grinnell ◽  
C.H. Ho ◽  
T.L. Tuan
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Adhesion ◽  
Binding Sites ◽  
Cell Spreading ◽  
The Other ◽  
Immunofluorescence Staining ◽  
Baby Hamster Kidney ◽  
Bhk Cells ◽  
Reducing Conditions ◽  
Latex Beads

In this report we describe cell adhesion and phagocytosis promoted by two monoclonal antibodies that were selected for immunofluorescence staining of non-permeabilized baby hamster kidney (BHK) cells. Anti-BHK1 staining was heaviest along cell margins, whereas anti-BHK2 staining was continuous along cell margins. Neither antibody stained elongated plaque structures such as were observed when cells were reacted with antibodies to fibronectin (FN) receptors. The monoclonal antibodies functioned as adhesion ligands in four different assays: attachment to culture dishes, spreading, binding of latex beads and phagocytosis. Anti-BHK1 and anti-BHK2 promoted attachment to culture dishes similarly, but anti-BHK2 was more effective at promoting cell spreading. Antibody-promoted cell spreading was inhibited by the peptides Ser-Asp-Gly-Arg and Gly-Arg-Gly-Asp-Ser-Pro but not by other, related, peptides tested. The monoclonal antibodies also promoted binding of latex beads, and the bead binding sites were motile, on the basis of their ‘capping’ response. Nevertheless, anti-BHK2 beads were phagocytosed by cells 5- to 20-fold more efficiently than anti-BHK1 beads. The binding sites for anti-BHK1 and anti-BHK2 were characterized by immunoprecipitation experiments. Anti-BHK1 binding sites contained 50K (K = 10(3) Mr) and 88K components under non-reducing conditions that migrated as a 51/53K doublet and a 93K component under reducing conditions. On the other hand, anti-BHK2 binding sites contained 88K and 110K components under non-reducing conditions that shifted to apparent 107K and 128K values when measured under reducing conditions.

GROWTH OF STAPHYLOCOCCUS AUREUS IN ACIDIFIED PASTEURIZED MILK1

1970 ◽  
Vol 33 (11) ◽  
pp. 516-520 ◽  
Author(s):  
T. E. Minor ◽  
E. H. Marth
Keyword(s):  
Staphylococcus Aureus ◽  
Acetic Acid ◽  
Lactic Acid ◽  
Hydrochloric Acid ◽  
Ph Value ◽  
The Other ◽  
Antagonistic Effects ◽  
Pasteurized Milk ◽  
Ph Values ◽  
Effect On Growth

The effect of gradually reducing the pH of pasteurized milk with acetic, citric, hydrochloric, lactic, and phosphoric acids over periods of 4, 8, and 12 hr on growth of Staphylococcus aureus 100 in this substrate was determined. In addition, 1: 1 mixtures of lactic acid and each of the other acids, and of acetic and citric acids were evaluated for their effect on growth of this organism. To achieve a 90% reduction in growth over a 12 hr period, a final pH value of 5.2 was required for acetic, 4.9 for lactic, 4.7 for phosphoric and citric, and 4.6 for hydrochloric acid. A 99% reduction during a 12 hr period was obtained with a final pH value of 5.0 for acetic, 4.6 for lactic, 4.5 for citric, 4.1 for phosphoric, and 4.0 for hydrochloric acid. A pH value of 3.3 was required for a 99.9% reduction with hydrochloric acid, whereas the same effect was produced at a pH value of 4.9 with acetic acid. Correspondingly lower pH values were required to inhibit growth within 8 and 4 hr periods. Mixtures of acids adjusted to pH values at the borderline for growth (12 hr period) exhibited neither synergistic nor antagonistic effects between two acids.

scholarly journals Demonstrating Pathogenicity of Enterobacter cloacae on Macadamia and Identifying Associated Volatiles of Gray Kernel of Macadamia in Hawaii

Plant Disease ◽  
2007 ◽  
Vol 91 (10) ◽  
pp. 1221-1228 ◽  
Author(s):  
K. A. Nishijima ◽  
M. M. Wall ◽  
M. S. Siderhurst
Keyword(s):  
Acetic Acid ◽  
Volatile Compounds ◽  
Enterobacter Cloacae ◽  
The Other ◽  
Biotic Factors ◽  
Macadamia Integrifolia ◽  
Abiotic And Biotic Factors ◽  
Foul Odor ◽  
Important Disease

Gray kernel is an important disease of macadamia (Macadamia integrifolia) that affects the quality of kernels, causing gray discoloration and a permeating, foul odor. Gray kernel symptoms were produced in raw, in-shell kernels of three cultivars of macadamia that were inoculated with strains of Enterobacter cloacae. Koch's postulates were fulfilled for three strains, demonstrating that E. cloacae is a causal agent of gray kernel. An inoculation protocol was developed to consistently reproduce gray kernel symptoms. Among the E. cloacae strains studied, macadamia strain LK 0802-3 and ginger strain B193-3 produced the highest incidences of disease (65 and 40%, respectively). The other macadamia strain, KN 04-2, produced gray kernel in 21.7% of inoculated nuts. Control treatments had 1.7% gray kernel symptoms. Some abiotic and biotic factors that affected incidence of gray kernel in inoculated kernels were identified. Volatiles of gray and nongray kernel samples also were analyzed. Ethanol and acetic acid were present in nongray and gray kernel samples, whereas volatiles from gray kernel samples included the additional compounds, 3-hydroxy-2-butanone (acetoin), 2,3-butanediol, phenol, and 2-methoxyphenol (guaiacol). This is believed to be the first report of the identification of volatile compounds associated with gray kernel.

Movement of Several Herbicides Through Excised Plant Tissue

Weed Science ◽  
1970 ◽  
Vol 18 (1) ◽  
pp. 64-68 ◽  
Author(s):  
T. D. Taylor ◽  
G. F. Warren
Keyword(s):  
Acetic Acid ◽  
Phaseolus Vulgaris ◽  
Plant Tissue ◽  
The Other ◽  
Tissue Orientation ◽  
Chemical Retention ◽  
Dichlorophenoxy Acetic Acid ◽  
Indole 3 Acetic Acid

Uptake and movement of various herbicides and auxins by bean (Phaseolus vulgarisL.) petiole sections were studied. Isopropylm-chlorocarbanilate (chlorpropham) was the most mobile of the compunds studied, followed in order of decreasing mobility by: indole-3-acetic acid (IAA), 3-amino-s-triazole (amitrole), (2,4-dichlorophenoxy)acetic acid (2,4-D), 3-(3,4-dichlorophenyl)-1-methoxy-1-methylurea (linuron), and 3-amino-2,5-dichlorobenzoic acid (amiben). Amiben immobilization may have been due to glucoside formation in the tissues. IAA was rapidly transported through basipetally but not acropetally oriented tissue. Tissue orientation had little effect on the movement of the other compounds. Mobility of the compounds studied, in general, appears to be a function of the amount of uncomplexed parent chemical. Retention is likely the result of conjugation with products in the cells or of physical binding in the cells.

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