Comparison of hemolysins of Vibrio cholerae non-O1 and Vibrio hollisae with thermostable direct hemolysin of Vibrio parahaemolyticus

1988 ◽  
Vol 34 (12) ◽  
pp. 1321-1324 ◽  
Author(s):  
Myonsun Yoh ◽  
Takeshi Honda ◽  
Toshio Miwatani
Keyword(s):  
Amino Acid ◽  
Vibrio Cholerae ◽  
Vibrio Parahaemolyticus ◽  
Antigenic Determinants ◽  
Amino Acid Compositions ◽  
Molecular Weights ◽  
Time Dependencies ◽  
Thermostable Direct Hemolysin ◽  
Effects Of Temperature ◽  
Vibrio Hollisae

Hemolysin (Vh-rTDH) produced by Vibrio hollisae and hemolysin (NAG-rTDH) produced by Vibrio cholerae non-O1 were characterized and compared with hemolysin (Vp-TDH) produced by Vibrio parahaemolyticus. These three hemolysins are each composed of two subunits and have similar, but not identical, molecular weights. The amino acid compositions of Vp-TDH and NAG-rTDH are similar, but are different from that of Vh-rTDH. The three hemolysins showed similar lethal toxicities to mice. The effects of temperature on hemolysis and the time dependencies of hemolysis by the three hemolysins were similar. The three were concluded to be immunologically related, but not identical, and to have common and also unique antigenic determinants.

scholarly journals α-Crystallin. Fractionation of subunits and sequence studies on an isolated polypeptide

1971 ◽  
Vol 124 (2) ◽  
pp. 345-355 ◽  
Author(s):  
Robert C. Augusteyn ◽  
Abraham Spector
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Cyanogen Bromide ◽  
Sodium Dodecyl ◽  
Deae Cellulose ◽  
Iodoacetic Acid ◽  
Cysteine Residue ◽  
Terminal Sequence ◽  
Amino Acid Compositions ◽  
Molecular Weights

α-Crystallin was carboxymethylated with radioactive iodoacetic acid in the presence of 7.6m-urea and then separated into six major fractions by chromatography on DEAE-cellulose in 7m-urea. Based on the amino acid compositions, specific radioactivities and sodium dodecyl sulphate–gel electrophoresis of the fractions, it was concluded that α-crystallin contains at least four different subunits: DU1A and DU1B, containing no cysteine; a third component represented by DU2B and DU3 containing one cysteine one cysteine residue per subunit; and DU4, which probably contains two residues of cysteine per subunit. Subunit DU1A was shown to be of sufficient purity for sequence studies. Cyanogen bromide cleavage yielded two peptides, CB-1 and CB-2, in approximately equal amounts as expected. The sum of the molecular weights and amino acid compositions of the peptides were both in excellent agreement with the results obtained for subunit DU1A. The amino acid sequence of the first sixteen residues of peptide CB-1 is: Ser-Leu-Thr-Lys-Asp-Phe-Asp-Glu-Val-Asn-Ile-Asp-Val-Ser-His-Phe-. The sequence of the first seventeen residues of peptide CB-2 is: Asp-Ile-Ala-Ile-Ser-His-Pro-Trp-Ile-Arg-Pro-Ser-Phe-Phe-Glu-Phe-His-. The N-terminal sequence of subunit DU1A was shown to be N-acetylmethionine followed by peptide CB-2.

scholarly journals Purified membrane and soluble folate binding proteins from cultured KB cells have similar amino acid compositions and molecular weights but differ in fatty acid acylation.

1987 ◽  
Vol 84 (18) ◽  
pp. 6546-6549 ◽  
Author(s):  
C. A. Luhrs ◽  
P. Pitiranggon ◽  
M. da Costa ◽  
S. P. Rothenberg ◽  
B. L. Slomiany ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Binding Proteins ◽  
Kb Cells ◽  
Amino Acid Compositions ◽  
Molecular Weights ◽  
Folate Binding Proteins ◽  
Similar Amino Acid

scholarly journals Interrelationship between cationic and anionic forms of glutathione S-transferases of bovine ocular lens

1980 ◽  
Vol 191 (1) ◽  
pp. 11-20 ◽  
Author(s):  
R P Saneto ◽  
Y C Awasthi ◽  
S K Srivastava
Keyword(s):  
Amino Acid ◽  
Glutathione Peroxidase ◽  
Vascular System ◽  
Liver Homogenate ◽  
Physiological Role ◽  
Antigenic Determinants ◽  
Ocular Lens ◽  
Glutathione S Transferase ◽  
Amino Acid Compositions ◽  
Bovine Lens

Since the eye is constantly exposed to potentially damaging chemical compounds present in the atmosphere and vascular system, we investigated the physiological role of glutathione S-transferase (GSH S-transferase) in detoxification mechanisms operative in the ocular lens. We have purified an anionic and a cationic GSH S-transferase from the bovine lens to homogeneity through a combination of gel filtration, ion-exchange and affinity chromatography. The anionic (pI 5.6) and cationic (pI 7.4) S-transferases were found to have distinct kinetic parameters (apparent Km and Vmax. pH optimum and energy of activation). However, both species were demonstrated to have similar molecular weights and amino acid compositions. Double-immunodiffusion and immunotitration studies showed that both lens S-transferases were immunologically similar. The very close similarity in amino acid compositions and immunological properties strongly indicates that these two transferases either originate from the same gene or at least share common antigenic determinants and originate from similar genes. The bovine lens GSH S-transferases had no glutathione peroxidase activity with either t-butyl hydroperoxide or cumene hydroperoxide as substrate. However, the antibody raised against the homogeneous anionic glutathione S-transferase from the bovine lens was found to precipitate both glutathione S-transferase and glutathione peroxidase activities out of solution in the supernatant of a crude bovine liver homogenate.

scholarly journals Isolation from a coastal fish of Vibrio hollisae capable of producing a hemolysin similar to the thermostable direct hemolysin of Vibrio parahaemolyticus.

1988 ◽  
Vol 54 (8) ◽  
pp. 2144-2146 ◽  
Author(s):  
M Nishibuchi ◽  
S Doke ◽  
S Toizumi ◽  
T Umeda ◽  
M Yoh ◽  
...  
Keyword(s):  
Vibrio Parahaemolyticus ◽  
Coastal Fish ◽  
Thermostable Direct Hemolysin ◽  
Vibrio Hollisae

scholarly journals Comparative amino acid sequence analysis of hemolysins produced by Vibrio hollisae and Vibrio parahaemolyticus.

1989 ◽  
Vol 171 (12) ◽  
pp. 6859-6861 ◽  
Author(s):  
M Yoh ◽  
T Honda ◽  
T Miwatani ◽  
S Tsunasawa ◽  
F Sakiyama
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Vibrio Parahaemolyticus ◽  
Amino Acid Sequence Analysis ◽  
Vibrio Hollisae

scholarly journals A comparison of the physical and chemical properties of four cytochromes c from Azotobacter vinelandii

1973 ◽  
Vol 135 (4) ◽  
pp. 617-630 ◽  
Author(s):  
Wilbur H. Campbell ◽  
William H. Orme-Johnson ◽  
Robert H. Burris
Keyword(s):  
Amino Acid ◽  
Spectral Properties ◽  
Azotobacter Vinelandii ◽  
Chemical Properties ◽  
Protein Cleavage ◽  
Separation And Purification ◽  
Amino Acid Compositions ◽  
Molecular Weights ◽  
Cytochromes C ◽  
Isoelectric Points

1. A modified method for the separation and purification of four cytochromes c from Azotobacter vinelandii is described. Two new cytochromes c have been purified and are designated cytochromes c(551) and c(555). 2. Additional evidence is presented to establish the dihaem nature of cytochrome c4. Ultracentrifugation data indicated similar molecular weights for the native and the denatured protein. Cleavage with CNBr yielded seven peptides; the amino acid compositions of the purified peptides were determined. Only one haem peptide was recovered. 3. Cytochromes c(551) and c(555) were characterized as acidic proteins of molecular weights about 12000. The spectral properties, isoelectric points, ‘maps’ of peptides from CNBr cleavage and amino acid compositions were determined for these two proteins. 4. The spectral properties, isoelectric points, molecular weights, CNBr peptide ‘maps’, amino acid compositions, relative oxidation–reduction potentials and e.p.r. (electron-paramagnetic-resonance) spectra of the four cytochromes c were compared. Cytochrome c4 and cytochrome c(551) appear to be distinct proteins. The distinction between cytochromes c5 and c(555) was not as clear, and our data are inadequate to establish firmly that they are distinct proteins. 5. The dihaem nature of cytochrome c4 is evident in its e.p.r. spectrum. The e.p.r. spectra are similar to the spectra of mammalian cytochromes c.

scholarly journals Comparison of the Heme Iron Utilization Systems of Pathogenic Vibrios

1999 ◽  
Vol 181 (11) ◽  
pp. 3594-3598 ◽  
Author(s):  
S. M. O’Malley ◽  
S. L. Mouton ◽  
D. A. Occhino ◽  
M. T. Deanda ◽  
J. R. Rashidi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Vibrio Cholerae ◽  
Protein Level ◽  
Vibrio Parahaemolyticus ◽  
Heme Iron ◽  
Chromosomal Dna ◽  
Vibrio Fluvialis ◽  
Pathogenic Vibrios ◽  
Iron Utilization

ABSTRACT Vibrio alginolyticus, Vibrio fluvialis, andVibrio parahaemolyticus utilized heme and hemoglobin as iron sources and contained chromosomal DNA similar to severalVibrio cholerae heme iron utilization genes. A V. parahaemolyticus gene that performed the function of V. cholerae hutA was isolated. A portion of the tonB1locus of V. parahaemolyticus was sequenced and found to encode proteins similar in amino acid sequence to V. cholerae HutW, TonB1, and ExbB1. A recombinant plasmid containing the V. cholerae tonB1 and exbB1D1 genes complemented a V. alginolyticus heme utilization mutant. These data suggest that the heme iron utilization systems of the pathogenic vibrios tested, particularly V. parahaemolyticusand V. alginolyticus, are similar at the DNA level, the functional level, and, in the case of V. parahaemolyticus, the amino acid sequence or protein level to that of V. cholerae.

scholarly journals PHYLOGENETIC ORIGINS OF ANTIBODY STRUCTURE

1966 ◽  
Vol 124 (5) ◽  
pp. 901-913 ◽  
Author(s):  
J. Marchalonis ◽  
G. M. Edelman
Keyword(s):  
Amino Acid ◽  
Animal Species ◽  
Single Injection ◽  
Light Chains ◽  
Amino Acid Compositions ◽  
Neutralizing Activity ◽  
Anuran Amphibian ◽  
Heavy Chains ◽  
Molecular Weights ◽  
Antibody Structure

The anuran amphibian, Rana catesbiana, has been found to possess at least two kinds of immunoglobulins corresponding to γG- and γM-classes. These classes have the same chain structures as those of their counterparts in higher animal species. Light chains of both immunoglobulins had molecular weights of 20,000. Heavy chains of the γM-class had molecular weights of 72,100; those of the γG-class had molecular weights of 53,600. The carbohydrate content of the γG-immunoglobulin was 2.1%, and that of the γM-protein was 10.8%. The amino acid compositions of the immunoglobulins were generally similar to those of mammalian immunoglobulins. After a single injection of phage antigen (f2), the order of appearance of phage-neutralizing activity in the frog immunoglobulin classes was (a) γM-antibodies, and (b) γG-antibodies. The results of this and previous studies suggest that the γG-immunoglobulins emerged at some point in evolution between the elasmobranchs and the anuran amphibians.

Purification and partial characterization of a Vibrio hollisae hemolysin that relates to the thermostable direct hemolysin of Vibrio parahaemolyticus

1986 ◽  
Vol 32 (8) ◽  
pp. 632-636 ◽  
Author(s):  
Myonsun Yoh ◽  
Takeshi Honda ◽  
Toshio Miwatani
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Vibrio Parahaemolyticus ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cross Reactivity ◽  
Diethylaminoethyl Cellulose ◽  
Dodecyl Sulfate ◽  
Thermostable Direct Hemolysin ◽  
Vibrio Hollisae

Hemolysin produced by Vibrio hollisae (Vh-rTDH), which is related to the thermostable direct hemolysin (Vp-TDH) of Vibrio parahaemolyticus, was studied. Vh-rTDH was purified by successive column chromatographies on diethylaminoethyl-cellulose and an immunoaffinity column coupled with anti Vp-TDH immunoglobulin. The purified toxin was homogeneous, as demonstrated by conventional and sodium dodecyl sulfate–polyacrylamide gel electrophoresis (PAGE). The molecular weight of Vh-rTDH was slightly smaller than that of Vp-TDH, as determined by sodium dodecyl sulfate – slab gel electrophoresis. Conventional PAGE also showed a difference between Vh-rTDH and Vp-TDH. Vp-TDH and Vh-rTDH showed different lytic activities on erythrocytes from various animals, in particular chicken, sheep, and calf. The hemolytic activity of Vh-rTDH was heat labile when heated at 70 °C for 10 min, unlike Vp-TDH. Immunological cross-reactivity between Vh-rTDH and Vp-TDH was demonstrated by both the Ouchterlony test and neutralization test.

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