scholarly journals Partial amino acid sequence of human pancreatic stone protein, a novel pancreatic secretory protein

1986 ◽  
Vol 238 (1) ◽  
pp. 227-232 ◽  
Author(s):  
G Montalto ◽  
J Bonicel ◽  
L Multigner ◽  
M Rovery ◽  
H Sarles ◽  
...  
Keyword(s):  
Amino Acid ◽  
Polypeptide Chain ◽  
Protein A ◽  
Protein Sequences ◽  
Secretory Protein ◽  
Molecular Characteristics ◽  
Pancreatic Stone Protein ◽  
Partial Amino Acid Sequence ◽  
Peptide Backbone ◽  
Pancreatic Stone

Pancreatic stone protein (PSP) is the major organic component of human pancreatic stones. With the use of monoclonal antibody immunoadsorbents, five immunoreactive forms (PSP-S) with close Mr values (14,000-19,000) were isolated from normal pancreatic juice. By CM-Trisacryl M chromatography the lowest-Mr form (PSP-S1) was separated from the others and some of its molecular characteristics were investigated. The Mr of the PSP-S1 polypeptide chain calculated from the amino acid composition was about 16,100. The N-terminal sequences (40 residues) of PSP and PSP-S1 are identical, which suggests that the peptide backbone is the same for both of these polypeptides. The PSP-S1 sequence was determined up to residue 65 and was found to be different from all other known protein sequences.

Pancreatic stone protein – A possible biomarker of multiorgan failure and mortality in children sepsis

Cytokine ◽  
2014 ◽  
Vol 66 (2) ◽  
pp. 106-111 ◽  
Author(s):  
Žurek Jiří ◽  
Michal Kýr ◽  
Martin Vavřina ◽  
Michal Fedora
Keyword(s):  
Multiorgan Failure ◽  
Protein A ◽  
Pancreatic Stone Protein ◽  
Pancreatic Stone

scholarly journals The occurrence in amino acid sequences of extensive informational symmetries based on possible codon-codon complementarity in the encoding polynucleotides

1976 ◽  
Vol 153 (3) ◽  
pp. 681-690 ◽  
Author(s):  
G M Polya ◽  
D R Phillips
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Basic Protein ◽  
Protein A ◽  
Protein Sequences ◽  
Amino Acid Sequences ◽  
Rat Skin ◽  
Skin Collagen ◽  
Low Probability

1. A procedure is described for the detection and assessment of informational complementarity in an amino acid sequence; it is based on possible autocomplementarity in the mRNA, and involves codon-to-codon matching. 2. This procedure was applied to myelin basic protein, a variety of protamines, histone IV, silk fibroin, rat skin collagen α1 chain and a sheep keratin. A multiplicity of extensive low-probability informational symmetries, based on codon-to-codon matching, were detected. 3. These low-probability orderings, which are independent of the actual mRNA codons, are rationalized in terms of the evolutionary ordering of the amino acid sequences concerned, in such a way that constraints on the secondary structure of the coding polynucleotides were satisfied. This possible interpretation is supported by a number of significant common properties of the protein sequences analysed.

scholarly journals Molecular Characteristics of VP1 Region of Enterovirus 71 Strains in China

2020 ◽  
Author(s):  
Haiyan Sun ◽  
Min Gao ◽  
Dawei Cui
Keyword(s):  
Amino Acid ◽  
Vaccine Strain ◽  
Repetitive Sequences ◽  
Protein A ◽  
Enterovirus 71 ◽  
Molecular Characteristics ◽  
Continuous Change ◽  
Amino Acid Homology ◽  
Genetic Characteristics ◽  
Vp1 Protein

Abstract Background Enterovirus 71 (EV71) is the most common causative agent of severe and fetal hand, foot, and mouth disease (HFMD) outbreaks worldwide, and the VP1 protein, a capsid protein of EV71, is responsible for the genotype of EV71, which is important for vaccine selection and effectiveness. We performed an observational study of the genetic characteristics and genotype of EV71 isolates in China. Methods The VP1 gene sequences of 3712 EV71 virus strains from China, excluding repetitive sequences, and 30 known EV71 genotypes, as reference strains, between 1986 and 2019 were obtained from GenBank. A phylogenetic tree, amino acid homology, genetic variation and genotype analysis of the EV71-VP1 protein were performed with MEGA 6.0 software. Results The amino acid identity of all Chinese EV71 strains was 88.33%-100%, 93.47%-100% with the vaccine strain H07, and 93.04%-100% with the vaccine strains FY7VP5 and FY-23K-B. Since 2000, the prevalent strains of EV71 were mainly the C4 genotype; the C4a subgenotype was predominant, the C4b subgenotype was the second, and other subgenotypes appeared sporadically between 2005 and 2018 in mainland China. The B4 genotype was the main genotype in Taiwan, and the epidemic strains were constantly changing. Some amino acid variations in VP1 of EV71 occurred with high frequencies: A289T (20.99%), H22Q (16.49%), A293S (15.95%), S283T (15.11%), V249I (7.76%), N31D (7.25%), and E98K (6.65%). Conclusion The C4 genotype of EV71 in China can match the vaccine, which can effectively control EV71 epidemiology. However, the efficacy of the vaccine strain is partially affected by the continuous change in epidemic strains in Taiwan, China. These studies suggested that the genetic characteristics of the EV71-VP1 region should be continuously monitored, which is critical for epidemic control and vaccine design against EV71 infection in children.

scholarly journals Characterization of collagenous and non-collagenous peptides of a glycoprotein isolated from alveoli of patients with alveolar proteinosis

1981 ◽  
Vol 193 (2) ◽  
pp. 447-457 ◽  
Author(s):  
S N Bhattacharyya
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Polypeptide Chain ◽  
Proteolytic Enzymes ◽  
Lung Lavage ◽  
Sequence Analyses ◽  
Partial Amino Acid Sequence ◽  
Pepsin Digestion ◽  
Alveolar Proteinosis

A glycoprotein of Mr 62 000 was isolated from lung lavage material of patients with alveolar proteinosis. The glycoprotein was found to contain (per molecule) 72 residues of glycine, 5 residues of hydroxyproline, 3 molecules of sialic acid, 4.9 molecules of mannose, 4.0 molecules of galactose, 0.9 molecule of fucose and 7.0 molecules of N-acetylglucosamine. Limited pepsin digestion of the glycoprotein resulted in six peptides, three of which contained hydroxyproline and nearly 30% glycine, and two of which contained all the carbohydrate present in the glycoprotein of Mr 62 000. The three peptides containing hydroxyproline and with high content of glycine contained a repeating -Gly-X-Y-sequence in the peptide chain. Partial amino acid-sequence analyses on the peptides derived from the digestion of the alveolar glycoprotein with various proteolytic enzymes indicate that this glycoprotein is characterized by the presence of alternating collagenous and non-collagenous regions in the same polypeptide chain.

scholarly journals A collagen-like amino acid sequence in a polypeptide chain of human C1q (a subcomponent of the first component of complement)

1974 ◽  
Vol 141 (1) ◽  
pp. 189-203 ◽  
Author(s):  
Kenneth B. M. Reid
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polypeptide Chain ◽  
Complete Sequence ◽  
Partial Amino Acid Sequence ◽  
Collagenase Digestion ◽  
A Chain

1. A partial amino acid sequence of 95 residues of the 191 residues in the oxidized A chain of human subcomponent C1q was determined. The partial nature of the sequence is because one overlapping peptide is missing in the proposed sequence, also the proof of some of the overlapping peptides depends partly on their amino acid composition and not on their complete sequence. 2. This region of the A chain contained a repeating sequence of glycine-X-Y (where X is often proline and Y is often hydroxyproline) for 78 residues. 3. The five hydroxylysine residues and the five hydroxyproline residues present in the oxidized A chain were all in these 78 residues and only in the Y position of the repeating sequence. 4. Prolonged collagenase digestion of the oxidized A chain yielded a large, apparently C-terminal, peptide which contained most of the non-collagenous sequences present in the chain. 5. It is concluded that there is a collagen-like region in the A chain of subcomponent C1q which constitutes most of the N-terminal half of the chain and that similar collagen-like regions will be found in the B and C chains.

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