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.

Characterization of the gene network driving the whole lung lavage (WLL) outcome in Pulmonary Alveolar Proteinosis (PAP).

2018 ◽  
Author(s):  
Michele Zorzetto ◽  
Francesco Bonella ◽  
Francesca Mariani ◽  
Elena Paracchini ◽  
Zamir Kadija ◽  
...  
Keyword(s):  
Gene Network ◽  
Pulmonary Alveolar Proteinosis ◽  
Lung Lavage ◽  
Whole Lung Lavage ◽  
Alveolar Proteinosis

scholarly journals Purification and Partial Characterization of Rat Fibrinogen (rat-Fbg)

1977 ◽  
Author(s):  
W. Nieuwenhuizen ◽  
Irina A.M. van Ruijven-Vermeer
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Proteolytic Enzymes ◽  
Mammalian Species ◽  
Rat Plasma ◽  
Gel Chromatography ◽  
Molecular Weights ◽  
Ammonium Sulphate Precipitation ◽  
Proteolytic Activities

Rat-Fbg was purified from rat plasma using Sepharose-1ysi ne chromatography, repeated ammonium sulphate precipitation (35% saturation) and gel chromatography on Sepharose 6B.In order to minimize proteolytic activity, rats were injected intravenously with Trasylol before bleeding, and the collected blood was treated with Trasylol and DFP.A preparation was obtained, which was 95% clottable and showed a single band on SDS-poly-acrylamide gel electrophoresis. Alanine was the only detectable am i no-term i na 1 amino acid.After reduction and modification of the SH groups the material could be separated into three distinct chains (Aα, Bβ and γ) by pore-limit Polyacrylamide slab-gel electrophoresis in sod i urn dodecyl sulphate. The amino acid composition of the whole Fbg and of the separated modified chains were determined. The molecular weights were 61,000, 58,000 and 51,000 for Aα, Bβ and γ-chains, respectively.In as far as the chains are concerned, our results are in contrast with the findings of Bouma et al. (J. Biol. Chem. 250(1975) 4678), who could not discriminate between Aα- and Bβ-chains in SDS-polyacry1 am i de gel electrophoresis. Evidence will be presented that this can be due to Aa-chain degradation caused by incomplete inhibition of proteolytic enzymes during the purification.It is concluded, that complete inhibition of proteolytic activities in all purification steps is essential to obtain native fibrinogen. Moreover, in contrast to the conclusions of Bouma rat-Fbg does not differ essentially from Fbg from other mammalian species.

Partial characterization of the heteropolysaccharide associated with the 7S domain of type IV collagen from placenta

1987 ◽  
Vol 65 (5) ◽  
pp. 501-506 ◽  
Author(s):  
James R. A. Leushner
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Chemical Analysis ◽  
Amino Acid Analysis ◽  
Molecular Sieve ◽  
Type Iv Collagen ◽  
Relative Mass ◽  
Type Iv ◽  
Structure Formula

A major heteropolysaccharide fraction was isolated from the 7S domain of human placental type IV collagen. Analyses revealed that it was an asparagine-linked oligosaccharide. Characterization using molecular sieve chromatography, exoglycosidase and endoglycosidase digestion, and chemical analysis suggested a bianternnary complex with the following structure:[Formula: see text]A microheterogeneity was noted with respect to the addition of the fucose and sialic acid residues. Analysis of component polypeptides of the 7S fraction following endoglycosidase treatment suggested that the most obvious site of heteropolysaccharide attachment was in a polypeptide of relative mass 40 000. Amino acid analysis of this isolated polypeptide indicated that it was rich in collagenous sequences and also contained half-cystine residues.

Partial amino acid sequence and characterization of a new BmK AS-like polypeptide from Chinese scorpion

Toxicon ◽  
1997 ◽  
Vol 35 (4) ◽  
pp. 492-493
Author(s):  
Y. Liu ◽  
H.-M. Ren ◽  
Q. Hu ◽  
J. Zhao ◽  
B.-L. Song ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Amino Acid Sequence

scholarly journals Chemical and hydrodynamic characterization of the human leucocyte receptor for complement subcomponent C1q

1989 ◽  
Vol 262 (2) ◽  
pp. 625-631 ◽  
Author(s):  
R Malhotra ◽  
R B Sim
Keyword(s):  
Amino Acid ◽  
Polypeptide Chain ◽  
Solid Phase ◽  
U937 Cells ◽  
Amino Acid Residues ◽  
Human Tonsil ◽  
Monocytic Cell ◽  
Monocytic Cell Line ◽  
Complement Component C3

A procedure for preparation of the receptor for complement subcomponent Clq from human tonsil lymphocytes and the monocytic cell line U937 was developed. The procedure is suitable for isolation of several hundred micrograms of the receptor, Clq-R, and has yielded sufficient material for chemical and hydrodynamic characterization. Clq-R from tonsil lymphocytes behaves identically with that from U937 cells. Clq-R has a monomer Mr of 56,000, and is an acidic glycoprotein containing about 17% carbohydrate. The polypeptide chain length is estimated to be 416-448 amino acid residues, with two or three sites for N-linked glycosylation. Detergent-solubilized Clq-R exists as an elongated dimer (f/fo = 1.8), and does not bind a significant weight of detergent. The radioiodinated isolated receptor binds specifically and saturably to solid-phase Clq, but not to collagen, IgG, bovine serum albumin or complement component C3.

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.

scholarly journals Characterization of Anammox Hydrazine Dehydrogenase, a Key N2-producing Enzyme in the Global Nitrogen Cycle

2016 ◽  
Vol 291 (33) ◽  
pp. 17077-17092 ◽  
Author(s):  
Wouter J. Maalcke ◽  
Joachim Reimann ◽  
Simon de Vries ◽  
Julea N. Butt ◽  
Andreas Dietl ◽  
...  
Keyword(s):  
Nitrous Oxide ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Changes ◽  
Catalytic Properties ◽  
Anammox Bacteria ◽  
Sequence Analyses ◽  
Denitrifying Microorganisms ◽  
Global Nitrogen Cycle

Anaerobic ammonium-oxidizing (anammox) bacteria derive their energy for growth from the oxidation of ammonium with nitrite as the electron acceptor. N2, the end product of this metabolism, is produced from the oxidation of the intermediate, hydrazine (N2H4). Previously, we identified N2-producing hydrazine dehydrogenase (KsHDH) from the anammox organism Kuenenia stuttgartiensis as the gene product of kustc0694 and determined some of its catalytic properties. In the genome of K. stuttgartiensis, kustc0694 is one of 10 paralogs related to octaheme hydroxylamine (NH2OH) oxidoreductase (HAO). Here, we characterized KsHDH as a covalently cross-linked homotrimeric octaheme protein as found for HAO and HAO-related hydroxylamine-oxidizing enzyme kustc1061 from K. stuttgartiensis. Interestingly, the HDH trimers formed octamers in solution, each octamer harboring an amazing 192 c-type heme moieties. Whereas HAO and kustc1061 are capable of hydrazine oxidation as well, KsHDH was highly specific for this activity. To understand this specificity, we performed detailed amino acid sequence analyses and investigated the catalytic and spectroscopic (electronic absorbance, EPR) properties of KsHDH in comparison with the well defined HAO and kustc1061. We conclude that HDH specificity is most likely derived from structural changes around the catalytic heme 4 (P460) and of the electron-wiring circuit comprising seven His/His-ligated c-type hemes in each subunit. These nuances make HDH a globally prominent N2-producing enzyme, next to nitrous oxide (N2O) reductase from denitrifying microorganisms.

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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