Association of a pH-sensitive peptide with membrane vesicles: role of amino acid sequence

Biochemistry ◽  
1990 ◽  
Vol 29 (37) ◽  
pp. 8713-8719 ◽  
Author(s):  
Roberta A. Parente ◽  
Laszlo Nadasdi ◽  
Nanda K. Subbarao ◽  
Francis C. Szoka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Membrane Vesicles ◽  
Ph Sensitive

scholarly journals Purification, characterization, gene sequence, and significance of a bacterioferritin from Mycobacterium leprae.

1994 ◽  
Vol 180 (1) ◽  
pp. 319-327 ◽  
Author(s):  
M C Pessolani ◽  
D R Smith ◽  
B Rivoire ◽  
J McCormick ◽  
S A Hefta ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Protein ◽  
Amino Acid Sequence ◽  
Mycobacterium Leprae ◽  
Native Molecular Mass ◽  
Molecular Features ◽  
Ferroxidase Center ◽  
Considerable Homology

The study of tissue-derived Mycobacterium leprae provides insights to the immunopathology of leprosy and helps identify broad molecular features necessary for mycobacterial parasitism. A major membrane protein (MMP-II) of in vivo-derived M. leprae previously recognized (Hunter, S.W., B. Rivoire, V. Mehra, B.R. Bloom, and P.J. Brennan. 1990. J. Biol. Chem. 265:14065) was purified from extracts of the organism and partial amino acid sequence obtained. This information allowed recognition, within one of the cosmids that encompass the entire M. leprae genome, of a complete gene, bfr, encoding a protein of subunit size 18.2 kD. The amino acid sequence deduced from the major membrane protein II (MMP-II) gene revealed considerable homology to several bacterioferritins. Analysis of the native protein demonstrated the iron content, absorption spectrum, and large native molecular mass (380 kD) of several known bacterioferritins. The ferroxidase-center residues typical of ferritins were conserved in the M. leprae product. Oligonucleotides derived from the amino acid sequence of M. leprae bacterioferritin enabled amplification of much of the MMP-II gene and the detection of homologous sequences in Mycobacterium paratuberculosis, Mycobacterium avium, Mycobacterium tuberculosis, Mycobacterium intracellulare, and Mycobacterium scrofulaceum. The role of this iron-rich protein in the virulence of M. leprae is discussed.

Expression of Na+-d-glucose cotransporter in brush-border membrane of the chicken intestine

1999 ◽  
Vol 276 (2) ◽  
pp. R627-R631 ◽  
Author(s):  
Carles Garriga ◽  
Nativitat Rovira ◽  
Miquel Moretó ◽  
Joana M. Planas
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Brush Border ◽  
Synthetic Peptide ◽  
Brush Border Membrane ◽  
Polyclonal Antibodies ◽  
Membrane Vesicles ◽  
Dependent Transport

We have studied the expression of Na+-d-glucose cotransporter in brush-border membrane vesicles (BBMVs) of chicken enterocytes to correlate the changes in the apical Na+-dependent transport with the changes in the amounts of transporter determined by Western blot analysis. Two different rabbit polyclonal antibodies were used simultaneously. The antibody raised against amino acids 564–575 of the deduced amino acid sequence of rabbit intestinal SGLT-1 ( antibody 1) specifically detects a single 75-kDa band in the three segments, and this band disappeared when the antibody was preabsorbed with the antigenic peptide. The antibody raised against the synthetic peptide corresponding to amino acids 402–420 of the same protein ( antibody 2) only reacts with jejunal and ileal samples, but no signal is found in BBMVs of rectum. Only when antibody 1 was used was there a linear correlation between the maximal transport rates of hexoses in BBMVs and the relative protein amounts determined by Western blot. These results indicate that the Na+-d-glucose cotransport in the jejunum, the ileum, and the rectum of chickens is due to an SGLT-1 type protein.

Critical role of an eight-amino acid sequence of VP1 in neutralization of poliovirus type 3

Nature ◽  
1983 ◽  
Vol 304 (5925) ◽  
pp. 459-462 ◽  
Author(s):  
D. M. A. Evans ◽  
P. D. Minor ◽  
G. S. Schild ◽  
J. W. Almond
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Critical Role ◽  
Poliovirus Type ◽  
Type 3

Anti-Mouse GPI-PLD Antisera Highlight Structural Differences between Murine and Bovine GPI-PLDs

2003 ◽  
Vol 384 (12) ◽  
pp. 1575-1582 ◽  
Author(s):  
P. Gregory ◽  
A. Ziemiecki ◽  
G. Zürcher ◽  
U. Brodbeck ◽  
P. Bütikofer
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase D ◽  
Mouse Liver ◽  
Physiological Role ◽  
Recombinant Enzyme ◽  
Short Peptide ◽  
Structural Differences

AbstractDespite its well characterised biochemistry, the physiological role of glycosylphosphatidylinositolspecific phospholipase D (GPIPLD) is unknown. Most of the previous studies investigating the distribution of GPI-PLD have focused on the human and bovine forms of the enzyme. Studies on mouse GPI-PLD are rare, partly due to the lack of a specific antimouse GPI-PLD antibody, but also due to the apparent low reactivity of existing antibodies to rodent GPI-PLDs. Here we describe the isolation of a mouse liver cDNA, the construction and expression of a recombinant enzyme and the generation of an affinitypurified rabbit antimouse GPI-PLD antiserum. The antibody shows good reactivity to partially purified murine and purified bovine GPI-PLD. In contrast, a rat antibovine GPI-PLD antibody shows no reactivity with the mouse enzyme and the two antibodies recognise different proteolytic fragments of the bovine enzyme. Comparison between the rodent, bovine and human enzymes indicates that small changes in the amino acid sequence of a short peptide in the mouse and bovine GPI-PLDs may contribute to the different reactivities of the two antisera. We discuss the implications of these results and stress the importance of antibody selection while investigating GPI-PLD in the mouse.

Amino acid sequence of a basic Agkistrodon halys blomhoffii phospholipase A2. Possible role of amino-terminal lysines in action on phospholipids of Escherichia coli

Biochemistry ◽  
1986 ◽  
Vol 25 (15) ◽  
pp. 4309-4314 ◽  
Author(s):  
Steven Forst ◽  
Jerrold Weiss ◽  
Peter Blackburn ◽  
Blas Frangione ◽  
Fernando Goni ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A2 ◽  
Amino Terminal

scholarly journals The Reverse Side of a Coin: “Factor-Free” Ribosomal Protein Synthesis In Vitro is a Consequence of the In Vivo Proofreading Mechanism

Biomolecules ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 588
Author(s):  
Finkelstein
Keyword(s):  
Quality Control ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ribosomal Protein ◽  
Elongation Factor ◽  
Ribosomal Protein Synthesis

This paper elucidates a close connection between two well-known facts that until now have seemed independent: (i) the quality control (“proofreading”) of the emerging amino acid sequence, occurring during the normal, elongation-factor-dependent ribosomal biosynthesis, which is performed by removing those Aa-tRNAs (aminoacyl tRNAs) whose anticodons are not complementary to the exhibited mRNA codons, and (ii) the in vitro discovered existence of the factor-free ribosomal synthesis of polypeptides. It is shown that a biological role of proofreading is played by a process that is exactly opposite to the step of factor-free binding of Aa-tRNA to the ribosome-exposed mRNA: a factor-free removal of that Aa-tRNA whose anticodon is not complementary to the ribosome-exhibited mRNA codon.

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