Application of heptapeptides containing D-amino acid residues immobilized to magnetic particles and Sepharose for the study of binding properties of gastric aspartic proteases

2012 ◽  
Vol 35 (15) ◽  
pp. 1899-1905 ◽  
Author(s):  
Michaela Rajčanová ◽  
Marie Tichá ◽  
Zdenka Kučerová
Keyword(s):  
Amino Acid ◽  
Magnetic Particles ◽  
Amino Acid Residues ◽  
Binding Properties ◽  
Aspartic Proteases

scholarly journals Amino acid residues conferring the nucleotide binding properties of N-acetyl-D-glucosamine 2-epimerase (renin binding protein)

2005 ◽  
Vol 26 (3) ◽  
pp. 117-121 ◽  
Author(s):  
Saori TAKAHASHI ◽  
Hironobu OGASAWARA ◽  
Kazuyuki HIWATASHI ◽  
Keishi HATA ◽  
Kazuyuki HORI ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Protein ◽  
Nucleotide Binding ◽  
Amino Acid Residues ◽  
Binding Properties

scholarly journals Alternative Splicing of the HumanRab6AGene Generates Two Close but Functionally Different Isoforms

2000 ◽  
Vol 11 (11) ◽  
pp. 3819-3833 ◽  
Author(s):  
Arnaud Echard ◽  
Frank J.M. Opdam ◽  
Hubert J.P.C. de Leeuw ◽  
Florence Jollivet ◽  
Paul Savelkoul ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Alternative Splicing ◽  
Amino Acid ◽  
Retrograde Transport ◽  
Amino Acid Substitutions ◽  
Amino Acid Residues ◽  
Binding Properties ◽  
Rab Protein ◽  
Gtp Binding ◽  
Functional Differences

Analysis of the human Rab6A gene structure reveals the presence of a duplicated exon, and incorporation of either of the two exons by alternative splicing is shown to generate two Rab6 isoforms named Rab6A and Rab6A′, which differ in only three amino acid residues located in regions flanking the PM3 GTP-binding domain of the proteins. These isoforms are ubiquitously expressed at similar levels, exhibit the same GTP-binding properties, and are localized to the Golgi apparatus. Overexpression of the GTP-bound mutants of Rab6A (Rab6A Q72L) or Rab6A′ (Rab6A′ Q72L) inhibits secretion in HeLa cells, but overexpression of Rab6A′ Q72L does not induce the redistribution of Golgi proteins into the endoplasmic reticulum. This suggests that Rab6A′ is not able to stimulate Golgi-to-endoplasmic reticulum retrograde transport, as described previously for Rab6A. In addition, Rab6A′ interacts with two Rab6A partners, GAPCenA and “clone 1,” but not with the kinesin-like protein Rabkinesin-6, a Golgi-associated Rab6A effector. Interestingly, we found that the functional differences between Rab6A and Rab6A′ are contingent on one amino acid (T or A at position 87). Therefore, limited amino acid substitutions within a Rab protein introduced by alternative splicing could represent a mechanism to generate functionally different isoforms that interact with distinct sets of effectors.

scholarly journals Binding Properties of Streptococcus gordonii SspA and SspB (Antigen I/II Family) Polypeptides Expressed on the Cell Surface of Lactococcus lactis MG1363

1998 ◽  
Vol 66 (10) ◽  
pp. 4633-4639 ◽  
Author(s):  
Ann R. Holmes ◽  
Christophe Gilbert ◽  
Jeremy M. Wells ◽  
Howard F. Jenkinson
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Lactococcus Lactis ◽  
Plasmid Vector ◽  
Surface Expression ◽  
Collagen Type I ◽  
Type I ◽  
Streptococcus Gordonii ◽  
Amino Acid Residues ◽  
Binding Properties

ABSTRACT The oral bacterium Streptococcus gordonii expresses two cell wall-associated polypeptides, designated SspA (1,542 amino acid residues) and SspB (1,462 amino acid residues), that have 70% sequence identity. These polypeptides are members of the antigen I/II family of oral streptococcal adhesins and mediate the binding of streptococci to salivary glycoproteins, collagen, and other oral microorganisms such as Actinomyces naeslundii. To determine if SspA and SspB have differential binding properties, the coding sequences of the sspA and sspB genes were cloned into expression plasmid vector pTREX1-usp45LS to generate pTREX1-sspA and pTREX1-sspB, respectively, and the Ssp polypeptides were displayed on the cell surface ofLactococcus lactis MG1363. Lactococcal cells expressing similar levels of surface SspA or SspB polypeptide were then compared for their abilities to adhere to a range of antigen I/II polypeptide substrates. More than twice as many L. lactis cells expressing SspA bound to immobilized salivary agglutinin glycoprotein (SAG) as did L. lactis cells expressing SspB. In contrast, lactococci expressing SspB adhered twice as well as lactococci producing SspA to collagen type I and toCandida albicans. The binding of A. naeslundiito lactococci was only weakly enhanced by surface expression of Ssp polypeptides. L. lactis(pTREX1-sspB) cells bound in greater numbers to SAG than did Enterococcus faecalis JH2-2 cells expressing SspB from pAM401EB-5. The results suggest that SspA and SspB have markedly different binding affinities for their oral substrates and thus may function to promote site diversity in colonization by S. gordonii.

scholarly journals Amino Acid Residues Conferring Ligand Binding Properties of Prostaglandin I and Prostaglandin D Receptors

2000 ◽  
Vol 275 (32) ◽  
pp. 24294-24303 ◽  
Author(s):  
Takuya Kobayashi ◽  
Fumitaka Ushikubi ◽  
Shuh Narumiya
Keyword(s):  
Amino Acid ◽  
Ligand Binding ◽  
Amino Acid Residues ◽  
Binding Properties

scholarly journals Interactions of Aβ1-42 Peptide and Its Three Fragments (Aβ8-12, Aβ8-13, and Aβ5-16) with Selected Nonsteroidal Drugs and Compounds of Natural Origin

Symmetry ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 1579
Author(s):  
Krzysztof Żamojć ◽  
Karolina Streńska ◽  
Dariusz Wyrzykowski ◽  
Lech Chmurzyński ◽  
Joanna Makowska
Keyword(s):  
Molecular Dynamics ◽  
Steady State ◽  
Amino Acid ◽  
Complex Formation ◽  
Amino Acid Residues ◽  
Binding Properties ◽  
Natural Origin ◽  
Steady State Fluorescence ◽  
The Stability ◽  
Steady State Fluorescence Spectroscopy

In the following paper, we present the results of our studies on the interactions of the Aβ1-42 peptide and its three short fragments, namely Aβ5-16 (RHDSGYEVHHQK; HZ1), Aβ8-13 (SGYEVH; HZ2), and Aβ8-12 (SGYEV; HZ3) with selected painkillers (ibuprofen and aspirin) and compounds of natural origin (anabasine and epinephrine). Steady-state fluorescence spectroscopy was used to study the binding properties of the selected systems. Additionally, based on molecular dynamics (MD) calculations supported by NMR-derived restrains, we have proposed the most likely area of the interactions of Aβ1-42 and Aβ5-16 peptides with the investigated compounds. The influence of symmetrically oriented side chains of amino acid residues present in the first part of the Aβ1-42 sequence on the stability of the resulting complexes has been discussed. Finally, the changes in the peptide structures on account of complex formation were analyzed.

scholarly journals Yeast acyl-CoA-binding protein: acyl-CoA-binding affinity and effect on intracellular acyl-CoA pool size

1994 ◽  
Vol 302 (2) ◽  
pp. 479-485 ◽  
Author(s):  
J Knudsen ◽  
N J Faergeman ◽  
H Skøtt ◽  
R Hummel ◽  
C Børsting ◽  
...  
Keyword(s):  
Amino Acid ◽  
Southern Blotting ◽  
Binding Protein ◽  
Amino Acid Residues ◽  
Binding Properties ◽  
High Affinity ◽  
Genes Encoding ◽  
The One

Acyl-CoA-binding protein (ACBP) is a 10 kDa protein characterized in vertebrates. We have isolated two ACBP homologues from the yeast Saccharomyces carlsbergensis, named yeast ACBP types 1 and 2. Both proteins contain 86 amino acid residues and are identical except for four conservative substitutions. In comparison with human ACBP, yeast ACBPs exhibit 48% (type 1) and 49% (type 2) conservation of amino acid residues. The amino acid sequence of S. carlsbergensis ACBP type 1 was found to be identical with the one ACBP present in Saccharomyces cerevisiae. A recombinant form of this protein was expressed in Escherichia coli and S. cerevisiae, purified, and its acyl-CoA-binding properties were characterized by isoelectric focusing and microcalorimetric analyses. The yeast ACBP was found to bind acyl-CoA esters with high affinity (Kd 0.55 x 10(-10) M). Overexpression of yeast ACBP in S. cerevisiae resulted in a significant expansion of the intracellular acyl-CoA pool. Finally, Southern-blotting analysis of the two genes encoding ACBP types 1 and 2 in S. carlsbergensis strongly indicated that this species is a hybrid between S. cerevisiae and Saccharomyces monacensis.

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