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

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

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.).

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.

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