Electrostatics and water occlusion regulate covalently‐bound FMN cofactors of Vibrio cholerae respiratory complex NQR

SummaryAfter thrombin treatment insolubilized fibrinmonomer, which is obtained from insolubilized fibrinogen covalently bound to agarose, adsorbs soluble fibrin and its derivatives from solutions. The immobilized proteins are attached to the agarose by the ‘A’ αchain. After reduction of the disulfide bridges the β and γchains can be removed from the agarose.After thrombin treatment the immobilized αchain adsorbs fibrinogen and fragment D. To some extent the β and γchain do not seem necessary for the adsorption. The amount adsorbed increases, when thrombin treatment of the insolubilized protein follows the reduction process.This may indicate that the fibrinopeptides ‘A’ of the insolubilized αchain are better accessible after the removal of the β and γchains.

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In vivo Production of Soluble Inorganic Pyrophosphatases in Two Strains of Vibrio cholerae

Bangladesh Journal of Microbiology ◽

10.3329/bjm.v24i1.1235 ◽

1970 ◽

Vol 24 (1) ◽

pp. 38-41

Author(s):

Taslima Taher Lina ◽

Mohammad Ilias

Keyword(s):

Vibrio Cholerae ◽

Specific Activity ◽

Experimental Conditions ◽

Environmental Strain ◽

Cell Extracts ◽

Atcc Strain ◽

The Family ◽

Effects Of Ph ◽

Vibrio Cholerae O1

The in vivo production of soluble inorganic pyrophosphatases (PPases) was investigated in two strains, namely, Vibrio cholerae EM 004 (environmental strain) and Vibrio cholerae O1 757 (ATCC strain). V. cholerae is known to contain both family I and family II PPase coding sequences. The production of family I and family II PPases were determined by measuring the enzyme activity in cell extracts. The effects of pH, temperature, salinity of the growth medium on the production of soluble PPases were studied. In case of family I PPase, V. cholerae EM 004 gave the highest specific activity at pH 9.0, with 2% NaCl + 0.011% NaF and at 37°C. The strain V. cholerae O1 757 gave the highest specific activity at pH 9.0, with media containing 0% NaCl and at 37°C. On the other hand, under all the conditions family II PPase did not give any significant specific activity, suggesting that the family II PPase was not produced in vivo in either strains of V. cholerae under different experimental conditions. Keywords: Vibrio cholerae, Pyrophosphatases (PPases), Specific activityDOI: http://dx.doi.org/10.3329/bjm.v24i1.1235 Bangladesh J Microbiol, Volume 24, Number 1, June 2007, pp 38-41

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INTERFERENCE BY SERUM PROTEINS WITH LH RADIOIMMUNOASSAY USING IMMUNOSORBENT

Acta Endocrinologica ◽

10.1530/acta.0.0720235 ◽

1973 ◽

Vol 72 (2) ◽

pp. 235-242 ◽

Cited By ~ 11

Author(s):

A. M. Reuter ◽

J. C. Hendrick ◽

J. Sulon ◽

P. Franchimont

Keyword(s):

Molecular Weight ◽

Human Serum ◽

High Molecular Weight ◽

Serum Proteins ◽

Void Volume ◽

High Molecular Weight Proteins ◽

Serum Fractionation ◽

Covalently Bound

ABSTRACT The percentage of LH* bound to antibodies that have been covalently bound to cellulose is diminished in the presence of LH-free human serum and sera from various species of animals. Serum fractionation studies on Sephadex G 200 show that the greatest interference comes from the proteins eluted in the void volume i. e. the high molecular weight proteins. Specifically, the gamma M globulins and the α2-macroglobulins appear to play an important role, as demonstrated by tests in which these proteins were neutralized by gamma M and α2-macroglobulin antisera.

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COMPARISON BETWEEN COVALENTLY BOUND AND FREE ANTIBODIES, USED FOR RADIOIMMUNOASSAY

Acta Endocrinologica ◽

10.1530/acta.0.0680425 ◽

1971 ◽

Vol 68 (3) ◽

pp. 425-430 ◽

Cited By ~ 11

Author(s):

J. Arends

Keyword(s):

Covalently Bound

ABSTRACT Radioimmunoassays using either free or covalently bound antibodies under otherwise identical conditions have been compared. A lowered utilization of antibodies and a loss in sensitivity protential have been observed with the last mentioned method.

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