scholarly journals Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion

Glycobiology ◽  
1995 ◽  
Vol 5 (4) ◽  
pp. 435-441 ◽  
Author(s):  
Heike Hall ◽  
Thomas Vorherr ◽  
Melitta Schachner
Keyword(s):  
Cell Adhesion ◽  
Amino Acid ◽  
Peptide Sequence ◽  
Carbohydrate Binding ◽  
Amino Acid Peptide

scholarly journals Angiogenesis Inhibition by a Short 13 Amino Acid Peptide Sequence of Tetrastatin, the α4(IV) NC1 Domain of Collagen IV

2020 ◽  
Vol 8 ◽  
Author(s):  
Alexia Vautrin-Glabik ◽  
Jérôme Devy ◽  
Camille Bour ◽  
Stéphanie Baud ◽  
Laurence Choulier ◽  
...  
Keyword(s):  
Amino Acid ◽  
Collagen Iv ◽  
Peptide Sequence ◽  
Angiogenesis Inhibition ◽  
Amino Acid Peptide ◽  
Nc1 Domain

scholarly journals The specificity of dipeptidyl aminopeptidase I (cathepsin C) and its use in peptide sequence studies

1972 ◽  
Vol 126 (3) ◽  
pp. 683-685 ◽  
Author(s):  
H. Lindley
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Peptide Sequence ◽  
Sequence Determination ◽  
Cathepsin C ◽  
The Third ◽  
Novel Technique ◽  
Dipeptidyl Aminopeptidase

1. The characterization of cathepsin C as an aminodipeptidase has been confirmed. 2. An extra limitation on its specificity, namely that peptides involving proline as the third residue are immune to the enzyme, has been found. 3. A novel technique of using the enzyme for amino acid sequence determination has been shown to be feasible.

scholarly journals Biochemical and Genetic Characterization of Mundticin KS, an Antilisterial Peptide Produced by Enterococcus mundtii NFRI 7393

2002 ◽  
Vol 68 (8) ◽  
pp. 3830-3840 ◽  
Author(s):  
Shinichi Kawamoto ◽  
Jun Shima ◽  
Rumi Sato ◽  
Tomoko Eguchi ◽  
Sadahiro Ohmomo ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Genetic Characterization ◽  
Solid Phase ◽  
Exchange Chromatography ◽  
Nucleotide Sequencing ◽  
Lactobacillus Curvatus ◽  
Amino Acid Peptide ◽  
Enterococcus Mundtii

ABSTRACT Mundticin KS, a bacteriocin produced by Enterococcus mundtii NFRI 7393 isolated from grass silage in Thailand, is active against closely related lactic acid bacteria and the food-borne pathogen Listeria monocytogenes. In this study, biochemical and genetic characterization of mundticin KS was done. Mundticin KS was purified to homogeneity by ammonium sulfate precipitation, sequential ion-exchange chromatography, and solid-phase extraction. The gene cluster (mun locus) for mundticin KS production was cloned, and DNA sequencing revealed that the mun locus consists of three genes, designated munA, munB, and munC. The munA gene encodes a 58-amino-acid mundticin KS precursor, munB encodes a protein of 674 amino acids involved in translocation and processing of the bacteriocin, and munC encodes a mundticin KS immunity protein of 98 amino acids. Amino acid and nucleotide sequencing revealed the complete, unambiguous primary structure of mundticin KS; mundticin KS comprises a 43-amino-acid peptide with an amino acid sequence similar to that of mundticin ATO6 produced by E. mundtii ATO6. Mundticin KS and mundticin ATO6 are distinguished by the inversion of the last two amino acids at their respective C termini. These two mundticins were expressed in Escherichia coli as recombinant peptides and found to be different in activity against certain Lactobacillus strains, such as Lactobacillus plantarum and Lactobacillus curvatus. Mundticin KS was successfully expressed by transformation with the recombinant plasmid containing the mun locus in heterogeneous hosts such as E. faecium, L. curvatus, and Lactococcus lactis. Based on our results, the mun locus is located on a 50-kb plasmid, pML1, of E. mundtii NFRI 7393.

scholarly journals Molecular characterization of the bovine <i>GHRL</i> gene (Short Communication)

2009 ◽  
Vol 52 (1) ◽  
pp. 79-84 ◽  
Author(s):  
F. G. Colinet ◽  
D. Portetelle ◽  
R. Renaville
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Short Communication ◽  
Hormone Secretion ◽  
Growth Hormone Secretion ◽  
Endogenous Ligand ◽  
Growth Hormone Secretagogue Receptor ◽  
Growth Hormone Secretagogue ◽  
Amino Acid Peptide

Abstract. Bovine ghrelin, a 27 amino acid peptide, has been identified in oxyntic glands of the abomasum. It is an endogenous ligand for growth hormone secretagogue receptor and stimulates food intake and growth hormone secretion. The bovine GHRL gene was completely sequenced and consists of five exons and four introns. Like mouse and human GHRL genes, we found that the bovine GHRL gene also contains a first non-coding exon of 21 bp. The bovine GHRL gene codes for 116 amino acid peptide named preproghrelin which contains the ghrelin peptide and another peptide similar to obestatin. Sequence analysis revealed eight polymorphisms, which are located in the non-coding sequence of the gene.

scholarly journals Characterization of Cichopeptins, New Phytotoxic Cyclic Lipodepsipeptides Produced by Pseudomonas cichorii SF1-54 and Their Role in Bacterial Midrib Rot Disease of Lettuce

2015 ◽  
Vol 28 (9) ◽  
pp. 1009-1022 ◽  
Author(s):  
Chien-Jui Huang ◽  
Ellen Pauwelyn ◽  
Marc Ongena ◽  
Delphine Debois ◽  
Valerie Leclère ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glycine Betaine ◽  
Sequence Similarity ◽  
Similar Rate ◽  
Peptide Sequence ◽  
Pseudomonas Cichorii ◽  
Cyclic Lipopeptides ◽  
Amino Acid Peptide ◽  
Fatty Acid Chain ◽  
Tomato Pathogen

The lettuce midrib rot pathogen Pseudomonas cichorii SF1-54 produces seven bioactive compounds with biosurfactant properties. Two compounds exhibited necrosis-inducing activity on chicory leaves. The structure of the two phytotoxic compounds, named cichopeptin A and B, was tentatively characterized. They are related cyclic lipopeptides composed of an unsaturated C12-fatty acid chain linked to the N-terminus of a 22–amino acid peptide moiety. Cichopeptin B differs from cichopeptin A only in the last C-terminal amino acid residue, which is probably Val instead of Leu/Ile. Based on peptide sequence similarity, cichopeptins are new cyclic lipopeptides related to corpeptin, produced by the tomato pathogen Pseudomonas corrugata. Production of cichopeptin is stimulated by glycine betaine but not by choline, an upstream precursor of glycine betaine. Furthermore, a gene cluster encoding cichopeptin synthethases, cipABCDEF, is responsible for cichopeptin biosynthesis. A cipA-deletion mutant exhibited significantly less virulence and rotten midribs than the parental strain upon spray inoculation on lettuce. However, the parental and mutant strains multiplied in lettuce leaves at a similar rate. These results demonstrate that cichopeptins contribute to virulence of P. cichorii SF1-54 on lettuce.

Modified-amino acid/peptide pyrimidine analogs: Synthesis, structural characterization and DFT study of N-(pyrimidyl) gabapentine and N-(pyrimidyl)baclofen

2021 ◽  
Author(s):  
Angel Garcia-Raso ◽  
ANGEL TERRON ◽  
JUAN J J FIOL ◽  
Adela Lopez-Zafra ◽  
Barbara Massanet ◽  
...  
Keyword(s):  
Amino Acid ◽  
Structural Characterization ◽  
Spectroscopic Characterization ◽  
Dft Study ◽  
Amino Acid Peptide ◽  
Pyrimidine Analogs

In this manuscript we report the synthesis and structural characterization of two new pyrimidine amino acid modified derivatives: N-(pyrimidyl)gabapentin (pyr-Gabapentin) (1) and N-(pyrimidyl)baclofen (pyr-baclofen) (2) and the spectroscopic characterization of...

scholarly journals Glycoinositol phospholipid anchor and protein C-terminus of bovine erythrocyte acetylcholinesterase: analysis by mass spectrometry and by protein and DNA sequencing

1996 ◽  
Vol 314 (3) ◽  
pp. 817-825 ◽  
Author(s):  
Robert HAAS ◽  
Brent C. JACKSON ◽  
Bruce REINHOLD ◽  
John D. FOSTER ◽  
Terrone L. ROSENBERRY
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Dna Sequencing ◽  
Protein Sequencing ◽  
Peptide Sequence ◽  
Partial Reduction ◽  
Bovine Erythrocyte ◽  
Gpi Anchor ◽  
Amino Acid Peptide ◽  
Fragmentation Patterns

Purified bovine erythrocyte acetylcholinesterase (AChE) was radiomethylated on its amine groups and incubated with bacterial phosphatidylinositol-specific phospholipase C to remove the lipid portion of the AChE glycoinositol phospholipid (GPI) anchor, and a C-terminal tryptic fragment that contained the residual GPI glycan was isolated by HPLC. Analysis by electrospray-ionization mass spectrometry revealed a parent ion of m/z 3798. The fragmentation patterns produced by collision-induced dissociation mass spectrometry of the +4 and +5 states of the parent ion indicated a 23-amino acid peptide in amide linkage to ethanolamine-PO4-Hex-Hex-Hex(PO4-ethanolamine) (HexNAc)-HexN(Me)2-inositol phosphate. The glycan structure is completely consistent with that obtained previously for the GPI anchor of human erythrocyte AChE except for the addition of the HexNAc substituent. A nearly complete peptide sequence was deduced from the fragmentation patterns, although four assignments were based only on single fragments of very low abundance. To resolve this uncertainty, a segment of bovine genomic DNA corresponding to the C-terminal AChE sequence was amplified by PCR. DNA sequencing established the 23-amino acid peptide sequence to be FLPKLLSATASEAPCTCSGPAHG, in agreement with the MS data and consistent with results from Edman protein sequencing. Dimerization of AChE polypeptides is mediated by intersubunit disulphide bonding in this C-terminal segment, but the bovine AChE contained two cysteine residues in a …CTC… motif, in contrast with human AChE which contains only a single cysteine in this segment. Although bovine AChE contained no free thiol groups reactive with iodo[14C]acetamide, partial reduction and alkylation with iodo[14C]acetamide revealed that conversion into monomers occurred with an overall incorporation of only one alkyl group per monomer. An identical level of alkylation was observed when dimeric human AChE was converted into monomers by partial reduction. The question of whether the bovine AChE contains one or two intersubunit disulphide linkages is considered.

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