Determination of Low Molecular weight Immunogenic Omp28 Protein and Gene of Salmonella typhimurium

2019 ◽  
Vol 8 (5) ◽  
pp. 172-177
Author(s):  
Rajeev Kumar ◽  
S. P. Singh ◽  
Mahesh Kumar ◽  
Anil Kumar
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Outer Membrane ◽  
Close Agreement ◽  
Outer Membrane Proteins ◽  
Low Molecular Weight ◽  
Predicted Amino Acid Sequence ◽  
Calculated Molecular Weight ◽  
Amplicon Size

Outer membrane of Gram-negative bacteria has complex profile of proteins. The outer membrane proteins (OMPs) isolated from S. typhimurium by urea-EDTA extraction method and analysed through SDS-PAGE showed a complex electrophoretic profile having more than 15 low molecular weight proteins with molecular masses ranging between 3.5 and 43 kDa. The most important outer membrane protein (Omp28) of S. typhimurium with submolecular masses of 12.32kDa of main protein was recovered. The gene responsible for expression of this protein was also amplified through PCR and sequenced, showed 341bp amplicon size and predicted amino acid sequence of this pro-tein was determined. The Antigenic index was calculated from amino acid sequence of same gene and found 2.2 (0.1-2.2) suggesting highly antigenic in nature. The experimentally determined values are close agreement with the theoretically calculated molecular weight 12.32 kDa and pI: 9.61 from the gene sequence of this protein. The antigenic natures of predicted protein values are close agreement with experimental determent of Omp28 of S. typhimurium a possible formula for vaccine developmental of genus Salmonella.

scholarly journals The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase

1989 ◽  
Vol 264 (5) ◽  
pp. 2560-2567
Author(s):  
G Camici ◽  
G Manao ◽  
G Cappugi ◽  
A Modesti ◽  
M Stefani ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Molecular Weight ◽  
Complete Amino Acid Sequence

scholarly journals The partial amino acid sequence of the major low molecular weight component of two human amyloid fibrils

FEBS Letters ◽  
1972 ◽  
Vol 22 (1) ◽  
pp. 121-123 ◽  
Author(s):  
Edward C. Franklin ◽  
Mordechai Pras ◽  
Mark Levin ◽  
Blas Frangione
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amyloid Fibrils ◽  
Low Molecular Weight ◽  
Partial Amino Acid Sequence

Variability of Low-Molecular-Weight, Heat-Modifiable Outer Membrane Proteins of Neisseria meningitidis

1980 ◽  
Vol 30 (3) ◽  
pp. 642-648
Author(s):  
J. T. Poolman ◽  
S. De Marie ◽  
H. C. Zanen
Keyword(s):  
Molecular Weight ◽  
Outer Membrane ◽  
High Molecular Weight ◽  
Outer Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Molecular Weights ◽  
Sds Page ◽  
Index Cases

Analysis of major outer membrane protein (MOMP) profiles of various meningococci by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (SDS-PAGE) revealed the presence of 0 to 2 low-molecular-weight, heat-modifiable MOMPs (molecular weight, 25,000 to 32,000) and 1 to 3 high-molecular-weight MOMPs (molecular weight, 32,000 to 46,000). Heat modifiability was investigated by comparing MOMP profiles after heating in SDS solutions at 100°C for 5 min or at 40°C for 1 h. Low-molecular-weight MOMPs shifted to higher apparent molecular weights after being heated at 100°C. Heat modifiability of high-molecular-weight MOMPs varied among strains; whenever modified these proteins shifted to lower apparent molecular weights after complete denaturation. Variability of low-molecular-weight, heat-modifiable MOMPs was demonstrated when MOMP profiles were compared of (i) isolates from index cases and associated cases and carriers among contacts, (ii) different isolates from the same individual, and (iii) isolates from a small epidemic caused by serogroup W-135. In some cases high-molecular-weight MOMPs revealed quantitative differences among related strains. The observed variability and quantitative differences indicate that MOMP serotyping and typing on the basis of SDS-PAGE profiles (PAGE typing) need careful reevaluation.

scholarly journals Characterization and Role of tbuX in Utilization of Toluene by Ralstonia pickettii PKO1

2000 ◽  
Vol 182 (5) ◽  
pp. 1232-1242 ◽  
Author(s):  
Hyung-Yeel Kahng ◽  
Armando M. Byrne ◽  
Ronald H. Olsen ◽  
Jerome J. Kukor
Keyword(s):  
Amino Acid ◽  
Outer Membrane ◽  
Stop Codon ◽  
Outer Membrane Proteins ◽  
Open Reading Frame ◽  
Predicted Amino Acid Sequence ◽  
Reading Frame ◽  
Ralstonia Pickettii ◽  
Degrading Bacteria

ABSTRACT The tbu regulon of Ralstonia pickettii PKO1 encodes enzymes involved in the catabolism of toluene, benzene, and related alkylaromatic hydrocarbons. The first operon in this regulon contains genes that encode the tbu pathway's initial catabolic enzyme, toluene-3-monooxygenase, as well as TbuT, the NtrC-like transcriptional activator for the entire regulon. It has been previously shown that the organization of tbuT, which is located immediately downstream of tbuA1UBVA2C, and the associated promoter (PtbuA1) is unique in that it results in a cascade type of up-regulation of tbuT in response to a variety of effector compounds. In our efforts to further characterize this unusual mode of gene regulation, we discovered another open reading frame, encoded on the strand opposite that of tbuT, 63 bp downstream of the tbuT stop codon. The 1,374-bp open reading frame, encoding a 458-amino-acid peptide, was designatedtbuX. The predicted amino acid sequence of TbuX exhibited significant similarity to several putative outer membrane proteins from aromatic hydrocarbon-degrading bacteria, as well as to FadL, an outer membrane protein needed for uptake of long-chain fatty acids inEscherichia coli. Based on sequence analysis, transcriptional and expression studies, and deletion analysis, TbuX seems to play an important role in the catabolism of toluene inR. pickettii PKO1. In addition, the expression oftbuX appears to be regulated in a manner such that low levels of TbuX are always present within the cell, whereas upon toluene exposure these levels dramatically increase, even more than those of toluene-3-monooxygenase. This expression pattern may relate to the possible role of TbuX as a facilitator of toluene entry into the cell.

The amino acid sequence of wheat β-purothionin

1976 ◽  
Vol 54 (10) ◽  
pp. 835-842 ◽  
Author(s):  
A. S. Mak ◽  
B. L. Jones
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Basic Protein ◽  
Viscum Album ◽  
Low Molecular Weight ◽  
Amino Acid Residues ◽  
Basic Proteins ◽  
Considerable Homology

The complete amino acid sequence of β-purothionin, a low molecular weight, very basic, protein isolated from wheat endosperm material, has been determined. β-purothionin is toxic to some bacteria, to yeasts, and to animals when injected. The protein contains 45 amino acid residues and has a molecular weight of 4913. The 8 cysteine and 10 basic residues are distributed throughout the molecule. The primary structure of the protein shows considerable homology to those of the viscotoxins, which are toxic, small, basic proteins found in the leaves and stems of European mistletoe (Viscum album L.).

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