scholarly journals Isolation and Characterization of a Novel Membrane Glycoprotein of 85000 Molecular Weight from Rat Liver Lysosomes.

1992 ◽  
Vol 40 (1) ◽  
pp. 170-173 ◽  
Author(s):  
Kenji AKASAKI ◽  
Hiroko KINOSHITA ◽  
Masataka FUKUZAWA ◽  
Makoto MAEDA ◽  
Yasunori YAMAGUCHI ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Rat Liver ◽  
Membrane Glycoprotein ◽  
Isolation And Characterization ◽  
Liver Lysosomes ◽  
Rat Liver Lysosomes

scholarly journals Studies on the permeability of rat liver lysosomes to carbohydrates

1969 ◽  
Vol 115 (4) ◽  
pp. 703-707 ◽  
Author(s):  
J B Lloyd
Keyword(s):  
Molecular Weight ◽  
Rat Liver ◽  
Substrate Concentration ◽  
Lysosomal Enzymes ◽  
Published Data ◽  
Progressive Loss ◽  
Liver Lysosomes ◽  
Before And After ◽  
Rat Liver Lysosomes ◽  
Free Activity

1. The latency of nitrocatechol sulphatase activity was measured in rat liver lysosomes before and after preincubation in 0·25m solutions of 25 different carbohydrates. 2. Preincubation in disaccharides, hexitols, gluconate, glucuronate or lactate gave little or no rise in ‘free’ sulphatase activity, indicating that these compounds do not easily penetrate the lysosomal membrane, but incubation in monosaccharides or the lower glycitols caused a progressive loss of latency. 3. Rates of increase in ‘free’ activity were taken as an indication of rates of solute penetration into lysosomes and were correlated with the structure and molecular weight of each sugar. 4. Additional evidence for non-penetration of maltose was obtained by demonstrating that the latency of lysosomal α-glucosidase is independent of substrate concentration employed. 5. The results are discussed in the light of published data on the latency of lysosomal enzymes.

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 a mannan-binding protein from rat liver.

1981 ◽  
Vol 256 (9) ◽  
pp. 4247-4252
Author(s):  
Y. Mizuno ◽  
Y. Kozutsumi ◽  
T. Kawasaki ◽  
I. Yamashina
Keyword(s):  
Rat Liver ◽  
Binding Protein ◽  
Isolation And Characterization
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