Characterization of Type-I NADH dehydrogenase. Polydispersity, molecular weight and polypeptide composition

1978 ◽  
Vol 501 (3) ◽  
pp. 458-469 ◽  
Author(s):  
G. Dooijewaard ◽  
G.J.M. De Bruin ◽  
P.J. Van Dijk ◽  
E.C. Slater
Keyword(s):  
Molecular Weight ◽  
Nadh Dehydrogenase ◽  
Type I ◽  
Polypeptide Composition

scholarly journals Extraction and Characterization of Collagen from Sand Sea Cucumber (Holothuria scabra)

2021 ◽  
Vol 26 (3) ◽  
pp. 319-327
Author(s):  
Gita Syahputra ◽  
Hariyatun Hariyatun ◽  
Muhammad Firdaus ◽  
Pugoh Santoso
Keyword(s):  
Molecular Weight ◽  
Sea Cucumber ◽  
Type I ◽  
Indonesian Seas ◽  
Holothuria Scabra ◽  
Aquatic Product ◽  
Electron Microscopy Analysis ◽  
Main Component ◽  
Almost All

Sand sea cucumber (Holothuria scabra) is an aquatic product that belongs to Echinodermata, a habitant in almost all Indonesian seas. The main component of the sea cucumber is protein, one of which is collagen. This study aimed to extract and characterize collagen from the species using the acid-base extraction method. The characterization of sea cucumber collagen includes molecular weight, amino acid components, Fourier transform infrared spectrophotometry, and scanning electron microscopy analysis. This study has successfully extracted collagen from the sample using an extraction system: NaOH 0.1 M; CH3COOH 0.1 M; and distilled water under 45°C treatments, gave 6% yield. The collagen has a molecular weight 110-130 kDa. Based on the infrared spectra, the specific functional groups of the collagen are amide A (3379.29 cm-1), amide B (2924.09 cm-1), amide I (1681.93 cm-1), amide II (1560.41 cm-1), and amide III (1249.87 cm-1). The collagen falls into type I. We suggest an alternative resource of collagen from sand sea cucumber, other than poultry and mammals.   Keywords: characterization, collagen, extraction, fishery, sand sea cucumber

scholarly journals Purification and Characterization of an Extracellular Poly(l-Lactic Acid) Depolymerase from a Soil Isolate,Amycolatopsis sp. Strain K104-1

2001 ◽  
Vol 67 (1) ◽  
pp. 345-353 ◽  
Author(s):  
Kohei Nakamura ◽  
Toshio Tomita ◽  
Naoki Abe ◽  
Yoshiyuki Kamio
Keyword(s):  
Molecular Weight ◽  
Lactic Acid ◽  
Collagen Type I ◽  
Type I ◽  
Chloromethyl Ketone ◽  
Diisopropyl Fluorophosphate ◽  
Soil Isolate ◽  
Solid Film ◽  
Subtilisin Inhibitor

ABSTRACT Poly(l-lactic acid) (PLA)-degradingAmycolatopsis sp. strains K104-1 and K104-2 were isolated by screening 300 soil samples for the ability to form clear zones on the PLA-emulsified mineral agar plates. Both of the strains assimilated >90% of emulsified 0.1% (wt/vol) PLA within 8 days under aerobic conditions. A novel PLA depolymerase with a molecular weight of 24,000 was purified to homogeneity from the culture supernatant of strain K104-1. The purified enzyme degraded high-molecular-weight PLA in emulsion and in solid film, ultimately forming lactic acid. The optimum pH for the enzyme activity was 9.5, and the optimum temperature was 55 to 60°C. The PLA depolymerase also degraded casein and fibrin but did not hydrolyze collagen type I, triolein, tributyrin, poly(β-hydroxybutyrate), or poly(ε-caprolactone). The PLA-degrading and caseinolytic activities of the enzyme were inhibited by diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride but were not significantly affected by soybean trypsin inhibitor,N-tosyl-l-lysyl chloromethyl ketone,N-tosyl-l-phenylalanyl chloromethyl ketone, and Streptomyces subtilisin inhibitor. Thus, Amycolatopsis sp. strain K104-1 excretes the unique PLA-degrading and fibrinolytic serine enzyme, utilizing extracellular polylactide as a sole carbon source.

Isolation and Characterization of Plasminogen Activator from Pig Leucocytes

1974 ◽  
Vol 31 (01) ◽  
pp. 072-085 ◽  
Author(s):  
M Kopitar ◽  
M Stegnar ◽  
B Accetto ◽  
D Lebez
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Ph Optimum ◽  
Isolation And Characterization ◽  
Ph Range ◽  
Inhibition Studies ◽  
Final Purification

SummaryPlasminogen activator was isolated from disrupted pig leucocytes by the aid of DEAE chromatography, gel filtration on Sephadex G-100 and final purification on CM cellulose, or by preparative gel electrophoresis.Isolated plasminogen activator corresponds No. 3 band of the starting sample of leucocyte cells (that is composed from 10 gel electrophoretic bands).pH optimum was found to be in pH range 8.0–8.5 and the highest pH stability is between pH range 5.0–8.0.Inhibition studies of isolated plasminogen activator were performed with EACA, AMCHA, PAMBA and Trasylol, using Anson and Astrup method. By Astrup method 100% inhibition was found with EACA and Trasylol and 30% with AMCHA. PAMBA gave 60% inhibition already at concentration 10–3 M/ml. Molecular weight of plasminogen activator was determined by gel filtration on Sephadex G-100. The value obtained from 4 different samples was found to be 28000–30500.

Studies on the Characterization of Factor VIII and a Co-factor VIII

1974 ◽  
Vol 31 (02) ◽  
pp. 328-338
Author(s):  
M. M. P Paulssen ◽  
H. L. M. A Vandenbussche-Scheffers ◽  
P. B Spaan ◽  
T de Jong ◽  
M. C Planje
Keyword(s):  
Molecular Weight ◽  
Factor Viii ◽  
The Body ◽  
Haemophilia A ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Polysaccharide Content ◽  
Plasma Factor ◽  
Two Factors

SummaryFactor VIII occurs in the body in two different forms. In lymph factor VIII is bound to chylomicra. In plasma, factor VIII is bound to a protein.After delipidation of chylomicra we obtained a glycoprotein with a high polysaccharide content and a molecular weight of approx. 160,000.In plasma, factor VIII is attached to a protein which is present in normal concentrations in plasma of patients with haemophilia A and in serum (co-factor VIII).This factor is deficient in both the plasma and the serum of patients with von Willebrand’s disease.The binding between factor VIII and co-factor VIII is reversible.Some properties of these two factors are described.

Rapid Isolation of High Molecular Weight Urokinase from Native Human Urine

1982 ◽  
Vol 47 (03) ◽  
pp. 197-202 ◽  
Author(s):  
Kurt Huber ◽  
Johannes Kirchheimer ◽  
Bernd R Binder
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Human Urine ◽  
Gel Filtration ◽  
Chain Structure ◽  
The Other ◽  
Single Chain ◽  
Apparent Homogeneity ◽  
Sequential Adsorption

SummaryUrokinase (UK) could be purified to apparent homogeneity starting from crude urine by sequential adsorption and elution of the enzyme to gelatine-Sepharose and agmatine-Sepharose followed by gel filtration on Sephadex G-150. The purified product exhibited characteristics of the high molecular weight urokinase (HMW-UK) but did contain two distinct entities, one of which exhibited a two chain structure as reported for the HMW-UK while the other one exhibited an apparent single chain structure. The purification described is rapid and simple and results in an enzyme with probably no major alterations. Yields are high enough to obtain purified enzymes for characterization of UK from individual donors.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

Removal of Hydrophobic and Hydrophilic Constituents by Anion Exchange Resin

1999 ◽  
Vol 40 (9) ◽  
pp. 207-214 ◽  
Author(s):  
J.-P. Croué ◽  
D. Violleau ◽  
C. Bodaire ◽  
B. Legube
Keyword(s):  
Molecular Weight ◽  
Anion Exchange ◽  
Water Source ◽  
Atomic Ratio ◽  
Size Exclusion ◽  
Salting Out ◽  
Anion Exchange Resins ◽  
Hydrophilic Character ◽  
Exchange Resins

The objective of this work was to compare the affinity of well characterized NOM fractions isolated from two surface waters with strong (gel matrix and macroporous matrix) and weak anion exchange resins (AER) using batch experiment conditions. The structural characterization of the fraction of NOM has shown that the higher the hydrophilic character, the lower the C/O atomic ratio, the lower the SUVA, the lower the aromatic carbon content and the lower the molecular weight. In general (not always), strong AER was more efficient to remove DOC than weak AER. For the same water source (Suwannee River), the higher the molecular weight of the NOM fraction, the lower the affinity with AER. Increasing the ionic strength favored the removal of the hydrophobic NOM fraction (“salting out” effect) while increasing the pH apparently reduced the removal of the hydrophilic NOM fraction. Results were discussed in terms of size exclusion, adsorption, anion exchange and also hydrophobic/hydrophilic repulsion.

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