The function of fimbriae in Myxococcus xanthus. I. Purification and properties of M. xanthus fimbriae

1979 ◽  
Vol 25 (10) ◽  
pp. 1152-1160 ◽  
Author(s):  
W. J. Dobson ◽  
H. D. McCurdy
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Amino Acid ◽  
Myxococcus Xanthus ◽  
Hydrolytic Enzymes ◽  
Antigenic Determinants ◽  
Freeze Thaw ◽  
Purification And Properties ◽  
Precise Relationship ◽  
Type Studies

Myxococcus xanthus fimbriae have been purified and characterized as part of a study of the function of fimbriae in this prokaryote. Myxococcus xanthus produced two types of fimbriae, termed flaccid (F) and rigid (R) on the basis of electron microscopy. F and R fimbriae differed slightly in their response to pH and freeze–thaw regimes but were similar in their resistance to hydrolytic enzymes, amino acid composition, molecular weight, carbohydrate content, and antigenic determinants. Although the precise relationship between F and R fimbriae is unknown, the possibility is considered that F fimbriae might represent a "contracted" form of the R type. Studies designed to determine fimbriae function in M. xanthus are described in an accompanying report.

scholarly journals Purification and Properties of Staphylocoagulase

1975 ◽  
Author(s):  
A.D. Muller ◽  
B. M. Bas ◽  
H. C. Hemker
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Aspartic Acid ◽  
Acid Composition ◽  
Isoelectric Point ◽  
Terminal Amino Acid ◽  
Purification And Properties ◽  
Terminal Amino

Staphylocoagulase, an exoprotein of coagulase positive staphylocoagulase, has been purified to a state in which only trace amounts of contaminating proteins are detectable.Purification was more than 35,000 fold, which is 7 times more than the highest value reported in the literature. The yield was about 15%.Aspartic acid was found as a single N-terminal amino acid in this preparation. The molecular weight is 61,000 and the isoelectric point lies at pH 4.53.The amino acid composition was determined.

scholarly journals The purification and properties of butyryl-coenzyme A dehydrogenase from Peptostreptococcus elsdenii

1971 ◽  
Vol 125 (3) ◽  
pp. 879-887 ◽  
Author(s):  
Paul C. Engel ◽  
V. Massey
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Simple Procedure ◽  
Potassium Bromide ◽  
Prosthetic Group ◽  
Pig Liver ◽  
Peak Absorption ◽  
Purification And Properties ◽  
Green Form ◽  
Spectrophotometric Titrations

Butyryl-CoA dehydrogenase prepared by a simple procedure from Peptostreptococcus elsdenii has a molecular weight of approx. 150000. The enzyme has FAD as its prosthetic group. The amino acid analysis is reported. This enzyme, like most of the corresponding mammalian ones, is green. The absorption band at 710nm can be abolished irreversibly by dithionite reduction and air reoxidation; it can be abolished reversibly by phenylmercuric acetate or potassium bromide. The enzyme as isolated appears to be a mixture of a green and a yellow form, both of which are active. This view is supported by the variable ‘greenness’ of different preparations and the biphasic curve obtained in anaerobic spectrophotometric titrations with dithionite. It can be calculated from the titration results that fully green enzyme would have a peak-to-peak absorption ratio (E710/E430) as great as 0.54. The green form is much less rapidly reduced by dithionite than the yellow form, but is nevertheless much more readily reduced by dithionite than the enzyme from pig liver. It is also more readily reoxidized by air and shows less tendency to form a semiquinone. Treatment with sodium borohydride produces an unusual reduced species that is probably the 3,4-dihydroflavin.

Purification and properties of a phenol carboxylic acid acyl esterase from Aspergillus flavus

1971 ◽  
Vol 17 (11) ◽  
pp. 1455-1463 ◽  
Author(s):  
J. J. Child ◽  
T. Oka ◽  
F. J. Simpson ◽  
H. G. Krishnamurty
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Carboxylic Acid ◽  
Aspergillus Flavus ◽  
Protocatechuic Acid ◽  
Hydroxybenzoic Acid ◽  
Purification And Properties ◽  
Wide Range ◽  
Hydrolysis Of ◽  
Active Preparation

Aspergillus flavus produces an extracellular esterase that hydrolyses phenolic carboxylic acid acyl esters. An assay based upon the measurement of the rate of release of phloroglucinol on hydrolysis of the ester of phloroglucinol and protocatechuic acid is described. The most active preparation hydrolyzed 30.8 μmoles of substrate per minute per milligram of protein and was active against a wide range of esters of meta and para hydroxybenzoic acid derivatives.The enzyme was isolated as a homogeneous protein, as judged by ultracentrifugation and by electrophoresis and had an isoelectric point of pH 4.45. The molecular weight was determined as 166 000. The enzyme is a glycoprotein containing 42.8% carbohydrate and the amino acid composition is described.

scholarly journals Colouring Matters of the Aphidoidea XLII. Purification and Properties of the Cyclising Enzyme [Protoaphin Dehydratase (Cyclising)] Concerned with Pigment Transformations in the Woolly Aphid Eriosoma lanigerum Hausmann (Hemiptera: Insecta)

1977 ◽  
Vol 30 (3) ◽  
pp. 173 ◽  
Author(s):  
DW Cameron ◽  
WH Sawyer ◽  
VM Trikojus
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Eriosoma Lanigerum ◽  
Purification And Properties ◽  
Woolly Aphid

Dried extracts of woolly aphid were treated with n-butanol, then by chromatography on DEAESephadex A50 and finally by filtration on Sephadex G150 to yield a substantially homogeneous protein catalysing the conversion of the aglucone of protoaphin into xanthoaphin. Traces of lowmolecular- weight contaminants were removed by chromatography on Sephadex G 100. The enzyme, which has a molecular weight of 120000�2000 and a high content of p-structure, was inhibited by naphthoresorcinol. Its glycoprotein nature was indicated by amino acid analysis.

scholarly journals Protein antigens of Streptococcus mutans: purification and properties of a double antigen and its protease-resistant component

1980 ◽  
Vol 28 (2) ◽  
pp. 486-493 ◽  
Author(s):  
M W Russell ◽  
L A Bergmeier ◽  
E D Zanders ◽  
T Lehner
Keyword(s):  
Molecular Weight ◽  
Physicochemical Properties ◽  
Streptococcus Mutans ◽  
Column Chromatography ◽  
Surface Protein ◽  
Peptide Chain ◽  
Antigenic Determinants ◽  
Protein Antigens ◽  
Purification And Properties ◽  
Culture Supernatants

A surface protein antigen of Streptococcus mutans having two sets of antigenic determinants (antigens I and II) was purified by column chromatography from culture supernatants of S. mutans serotype c. The protease-resistant component, antigen II, was purified from pronase-digested antigen I/II. The antigens were analyzed chemically and immunologically, and their physicochemical properties were investigated. Antigen I/II consisted of more than 80% protein, and its peptide chain molecular weight was estimated to be 185,000. Antigen II consisted of approximately 60% protein, with a peptide chain molecular weight of 48,000. Antisera to antigens I/II and II were raised in rabbits and used to investigate the presence of the antigens in cells of other streptococci. This indicated that not only serotype c but also serotypes e and f possessed antigen I and II determinants, whereas serotypes a, d, and g possessed a determinant related to antigen I but not one related to antigen II.

scholarly journals Purification and properties of the nicotinamide–adenine dinucleotide phosphate-dependent isocitrate dehydrogenase from pig liver cytoplasm

1970 ◽  
Vol 118 (2) ◽  
pp. 253-258 ◽  
Author(s):  
J. A. Illingworth ◽  
K. F. Tipton
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Isocitrate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Soluble Fraction ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Turnover Number ◽  
Pig Liver ◽  
Extinction Coefficients ◽  
Purification And Properties

The NADP-dependent isocitrate dehydrogenase from pig liver soluble fraction was purified over 500-fold with an overall yield of 25%. The purified enzyme, which is homogeneous by all the usual criteria, has a molecular weight of about 75000 and is composed of two identical subunits. This has been demonstrated by ultracentrifugation, fluorescence titration and peptide `fingerprinting'. The maximal turnover number, extinction coefficients at 280nm and 260nm and amino acid analysis are described.

Acetylcholinesterase aus dem Gift von Bungarus multicinctus. Reinigung und Eigenschaften/The Acetylcholinesterase of Bungarus multicinctus Venom. Purification and Properties

1979 ◽  
Vol 34 (1-2) ◽  
pp. 27-32 ◽  
Author(s):  
H. Großmann ◽  
M. Weinert ◽  
M. Liefländer
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Amino Acid Analysis ◽  
Specific Activity ◽  
Terminal Amino Acid ◽  
Purification And Properties ◽  
Gradient Gel Electrophoresis ◽  
Terminal Amino

Abstract Acetylcholinesterase from Banded krait (Bungarus multicinctus) venom has been purified by CM-Sephadex chromatography and affinity chromatography to a specific activity of 4290 U/mg. The purified enzyme is a glycoprotein. It is free of electrophoretically detectable contaminating proteins. A molecular weight of 140 000 ± 5 000 has been determined by gradient gel electrophoresis for the native enzyme. It is split into two equal-sized subunits (Mr 70 000 ± 2 000) by SDS treatment. The N-terminal amino acid analysis gave glycine and serine. The purified acetyl­ cholinesterase can be resolved by disc gel electrophoresis into four and by isoelectric focusing into six isozymes. The pI value of the main isozyme has been found to be 5.98 ± 0.05.

Structural study on liver gelactin

1984 ◽  
Vol 62 (11) ◽  
pp. 1072-1075 ◽  
Author(s):  
Julian Gruda ◽  
Hélène-Marie Thérien
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Structural Study ◽  
Isoelectric Focusing ◽  
Isoelectric Point ◽  
Gel Filtration ◽  
Rabbit Liver

Electron microscopy, ultracentrifugation, gel filtration, and isoelectric focusing were carried out with gelactin, an actin-gelling protein from rabbit liver. Gelactin is a dimeric acidic protein (isoelectric point (pI) = 5.45), with a molecular weight of 190 000, a Svedberg constant of 6.25, and a Stoke's radius and length of 7.0 and 28 nm, respectively. While different from α-actinin by pI and amino acid composition, gelactin belongs by its dimensions to the class of α-actinins.

Purification and Properties of Bovine Pituitary Renin

1982 ◽  
Vol 63 (s8) ◽  
pp. 179s-181s
Author(s):  
Tamiko Ohsawa ◽  
Shigehisa Hirose ◽  
Tadashi Inagami ◽  
Kazuo Murakami
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Anterior Pituitary ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Purification And Properties ◽  
Antigenic Properties ◽  
Hog Kidney

1. Renin was purified to homogeneity from bovine anterior pituitary by using batchwise DEAE-cellulose chromatography, pepstatin-aminohexyl-agarose affinity chromatography, Ultrogel AcA 44 gel filtration and DEAE-Sephacel and CM-cellulose ion exchange chromatography. 2. The enzyme has a molecular weight of 36 000 and an isoelectric point of 5.25, and exhibits optimum activity at a pH between 6.5 and 7.5. 3. The amino acid composition and antigenic properties of this purified renin are very similar to those of rat, dog and hog kidney renins.

Evaluation of the dark field method for large association of spread DNA

1978 ◽  
Vol 36 (2) ◽  
pp. 190-191
Author(s):  
Douglas C. Barker
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Mitochondrial Dna ◽  
Extraction Method ◽  
Field Method ◽  
Dark Field ◽  
Kinetoplast Dna ◽  
Field Electron ◽  
Field Electron Microscopy ◽  
Dark Field Electron

A number of satisfactory methods are available for the electron microscopy of nicleic acids. These methods concentrated on fragments of nuclear, viral and mitochondrial DNA less than 50 megadaltons, on denaturation and heteroduplex mapping (Davies et al 1971) or on the interaction between proteins and DNA (Brack and Delain 1975). Less attention has been paid to the experimental criteria necessary for spreading and visualisation by dark field electron microscopy of large intact issociations of DNA. This communication will report on those criteria in relation to the ultrastructure of the (approx. 1 x 10-14g) DNA component of the kinetoplast from Trypanosomes. An extraction method has been developed to eliminate native endonucleases and nuclear contamination and to isolate the kinetoplast DNA (KDNA) as a compact network of high molecular weight. In collaboration with Dr. Ch. Brack (Basel [nstitute of Immunology), we studied the conditions necessary to prepare this KDNA Tor dark field electron microscopy using the microdrop spreading technique.

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