scholarly journals The Blocked Amino-Terminal Peptide of Feather Keratin

1971 ◽  
Vol 24 (1) ◽  
pp. 179 ◽  
Author(s):  
IJ O'donnell
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Amino Groups ◽  
Amino Terminal ◽  
Acetyl Content ◽  
Electrophoretic Patterns ◽  
Isolation And Characterization ◽  
Primary Amino

Proteins extracted from reduced and carboxymethylated feather keratins (SCM-keratins) have been studied by Harrap and Woods (1964a, 1964b, 1967). They have demonstrated the presence of electrophoretic heterogeneity amongst the proteins and have obtained a molecular weight of approximately 11,000 in agreement with earlier work of Woodin (1954). There was no indication of marked heterogeneity with respect to size. Using acid hydrolysis and determination of acetic acid produced they found an acetyl content of 1 �30 molesj104 g in the rachis off owl feathers. These were thought to be attached to primary amino groups since there were no O-acetyl groups. In the present paper the isolation and characterization of the predominant, and probably sole, amino-terminal tripeptide from goose feather calamus is described. Goose feather calamus was chosen because its extracted proteins had one of the simplest electrophoretic patterns of proteins from the feathers of a number of species (Harrap and Woods 1967).

Isolierung und Charakterisierung einer Acetylester-Hydrolase aus Aspergillus rtiger / Isolation and Characterization of an Acetylester-Hydrolase from Aspergillus niger

1980 ◽  
Vol 35 (9-10) ◽  
pp. 696-698 ◽  
Author(s):  
B. Schöbel ◽  
W. Pollmann
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Temperature Optimum ◽  
Isolation And Characterization ◽  
Glyceryl Triacetate ◽  
Characteristic Features ◽  
The Stability ◽  
Acetic Acid Esters ◽  
Acid Esters

Abstract The characteristic features of an acetic acid esters hydrolyzing enzyme (acetylesterase, EC 3.1.1.16) are described. The pH- and temperature optimum were 7.0 and 40 °C respectively. The stability of the enzyme regarding different pH- and temperature conditions was investigated. The molecular weight of the acetylesterase could be determined to 160000. A small acetic ester hydrolyzing activity was found too with a molecular weight of about 25000. The activity was not inhibited by addition of di-isopropylphosphorofluoridate (DFP) or physostigmine. The KM-value for glyceryl triacetate was about 90 mM. Concentration of the enzyme was done by ultrafiltration and column-chromatography. The enzymatic activity tests were performed titrimetrically using glyceryl triacetate for substrate.

POLYMERS OF AMINOACETALDEHYDE

1945 ◽  
Vol 23b (4) ◽  
pp. 158-163
Author(s):  
H. H. Richmond ◽  
George F. Wright
Keyword(s):  
Molecular Weight ◽  
Ammonium Chloride ◽  
Ammonium Carbonate ◽  
Hydroxyl Groups ◽  
Molecular Weight Determination ◽  
Amino Groups ◽  
Primary Amino

The compound designated by Emil Fischer as 2,5-dihydroxypiperazine has been shown to be tris-aminomethyltrioxane by molecular weight determination of its derivatives. These benzoyl and benzenesulphonyl chloride derivatives further demonstrate the absence of hydroxyl groups and the presence of primary amino groups in the original compound. It has been found that use of ammonium carbonate, but not ammonium chloride, enhances the yield of aminoacetal obtained by ammonolysis of chloroacetal.

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.

Preparation and Characterization of the High Molecular Weight [3H]Hyaluronic Acid

1992 ◽  
Vol 57 (10) ◽  
pp. 2151-2156 ◽  
Author(s):  
Peter Chabreček ◽  
Ladislav Šoltés ◽  
Hynek Hradec ◽  
Jiří Filip ◽  
Eduard Orviský
Keyword(s):  
Molecular Weight ◽  
Hyaluronic Acid ◽  
High Molecular Weight ◽  
Methyl Bromide ◽  
High Performance ◽  
Hydrogen Atoms ◽  
Isolation And Characterization ◽  
Labelling Procedure ◽  
Enzymatic Depolymerization

Two methods for the preparation of high molecular weight [3H]hyaluronic acid were investigated. In the first one, hydrogen atoms in the molecule were replaced by tritium. This isotopic substitution was performed in aqueous solution using Pd/CaCO3 as the catalyst. In the second method, the high molecular weight hyaluronic acid was alkylated with [3H]methyl bromide in liquid ammonia at a temperature of -33.5 °C. High-performance gel permeation chromatographic separation method was used for the isolation and characterization of the high molecular weight [3H]hyaluronic acid. Molecular weight parameters for the labelled biopolymers were Mw = 128 kDa, Mw/Mn = 1.88 (first method) and Mw = 268 kDa, Mw/Mn = 1.55 (second method). The high molecular weight [3H]hyaluronic acid having Mw = 268 kDa was degraded further by specific hyaluronidase. Products of the enzymatic depolymerization were observed to be identical for both, labelled and cold biopolymer. This finding indicates that the described labelling procedure using [3H]methyl bromide does not induce any major structural rearrangements in the molecule.

scholarly journals Isolation and characterization of pathogenic Escherichia coli bacteriophages from chicken and beef offal

2020 ◽  
Vol 13 (1) ◽  
Author(s):  
Celosia Lukman ◽  
Christopher Yonathan ◽  
Stella Magdalena ◽  
Diana Elizabeth Waturangi
Keyword(s):  
Escherichia Coli ◽  
Foodborne Pathogens ◽  
High Efficiency ◽  
Multiplicity Of Infection ◽  
Isolation And Characterization ◽  
Transmission Electron ◽  
Pathogenic Escherichia Coli ◽  
Family Based

Abstract Objective This study was conducted to isolate and characterize lytic bacteriophages for pathogenic Escherichia coli from chicken and beef offal, and analyze their capability as biocontrol for several foodborne pathogens. Methods done in this research are bacteriophage isolation, purification, titer determination, application, determination of host range and minimum multiplicity of infection (miMOI), and bacteriophage morphology. Results Six bacteriophages successfully isolated from chicken and beef offal using EPEC and EHEC as host strain. Bacteriophage titers observed between 109 and 1010 PFU mL−1. CS EPEC and BL EHEC bacteriophage showed high efficiency in reduction of EPEC or EHEC contamination in meat about 99.20% and 99.04%. The lowest miMOI was 0.01 showed by CS EPEC bacteriophage. CI EPEC and BL EPEC bacteriophage suspected as Myoviridae family based on its micrograph from Transmission Electron Microscopy (TEM). Refers to their activity, bacteriophages isolated in this study have a great potential to be used as biocontrol against several foodborne pathogens.

scholarly journals Characterization of a Novel Fructosyltransferase from Lactobacillus reuteri That Synthesizes High-Molecular-Weight Inulin and Inulin Oligosaccharides

2002 ◽  
Vol 68 (9) ◽  
pp. 4390-4398 ◽  
Author(s):  
S. A. F. T. van Hijum ◽  
G. H. van Geel-Schutten ◽  
H. Rahaoui ◽  
M. J. E. C. van der Maarel ◽  
L. Dijkhuizen
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Lactobacillus Reuteri ◽  
Bacterial Strains ◽  
Potential Health ◽  
Isolation And Characterization ◽  
A Cell ◽  
Encoding Gene ◽  
First Time

ABSTRACT Fructosyltransferase (FTF) enzymes produce fructose polymers (fructans) from sucrose. Here, we report the isolation and characterization of an FTF-encoding gene from Lactobacillus reuteri strain 121. A C-terminally truncated version of the ftf gene was successfully expressed in Escherichia coli. When incubated with sucrose, the purified recombinant FTF enzyme produced large amounts of fructo-oligosaccharides (FOS) with β-(2→1)-linked fructosyl units, plus a high-molecular-weight fructan polymer (>107) with β-(2→1) linkages (an inulin). FOS, but not inulin, was found in supernatants of L. reuteri strain 121 cultures grown on medium containing sucrose. Bacterial inulin production has been reported for only Streptococcus mutans strains. FOS production has been reported for a few bacterial strains. This paper reports the first-time isolation and molecular characterization of (i) a Lactobacillus ftf gene, (ii) an inulosucrase associated with a generally regarded as safe bacterium, (iii) an FTF enzyme synthesizing both a high molecular weight inulin and FOS, and (iv) an FTF protein containing a cell wall-anchoring LPXTG motif. The biological relevance and potential health benefits of an inulosucrase associated with an L. reuteri strain remain to be established.

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