The identification of a barley haze active protein that influences beer haze stability: Cloning and characterisation of the barley SE protein as a barley trypsin inhibitor of the chloroform/methanol type

2007 ◽  
Vol 45 (3) ◽  
pp. 343-352 ◽  
Author(s):  
Louise H. Robinson ◽  
Juan Juttner ◽  
Andrew Milligan ◽  
Jelle Lahnstein ◽  
Jason K. Eglinton ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Active Protein ◽  
Chloroform Methanol ◽  
Barley Trypsin Inhibitor

Influence of the carbohydrate moiety on rotational correlation time and hydrodynamic volume of cow colostrum trypsin inhibitor

1985 ◽  
Vol 50 (1) ◽  
pp. 146-152
Author(s):  
Petr Štrop ◽  
Věra Jonáková
Keyword(s):  
Trypsin Inhibitor ◽  
Correlation Time ◽  
Gel Permeation Chromatography ◽  
Rotational Correlation Time ◽  
Active Protein ◽  
Fluorescence Depolarization ◽  
Kunitz Inhibitor ◽  
Rotational Correlation Times ◽  
The Mean ◽  
Rotational Correlation

A large polysaccharide moiety of the cow colostrum trypsin inhibitor was removed by enzymatic cleavage; fully active protein was obtained by affinity chromatography. Rotational correlation times of the inhibitor labelled by dansyl chloride obtained from fluorescence depolarization measurements and hydrodynamic volumes from gel-permeation chromatography for protein with and without polysaccharide were compared with those of homologous Kunitz inhibitor. The mean rotational correlation time 105 ns and apparent mol. weight 16 000 were obtained for the colostrum inhibitor with polysaccharides; these values are considerably reduced to 44 ns and 8 700 dalton after removal of the polysaccharide moiety. For the pancreatic inhibitor an about four times shorter correlation time of 24 ns was obtained.

The role of the N34S mutation in the trypsin inhibitor gene SPINK1 in patients with chronic pancreatitis from Romania

2009 ◽  
Vol 47 (06) ◽  
Author(s):  
B Diaconu ◽  
A Schneider ◽  
R Pfützer ◽  
T Mocan ◽  
M Scăfaru ◽  
...  
Keyword(s):  
Chronic Pancreatitis ◽  
Trypsin Inhibitor ◽  
N34s Mutation ◽  
Inhibitor Gene

Half-Life of Platelet Factor 4 (PF-4) in Plasma and Platelets from Macaca Mulatta

1977 ◽  
Vol 37 (01) ◽  
pp. 073-080 ◽  
Author(s):  
Knut Gjesdal ◽  
Duncan S. Pepper
Keyword(s):  
Macaca Mulatta ◽  
Half Life ◽  
Human Platelet ◽  
Gel Filtration ◽  
Platelet Factor 4 ◽  
Active Protein ◽  
Platelet Factor ◽  
Membrane Bound

SummaryHuman platelet factor 4 (PF-4) showed a reaction of complete identity with PF-4 from Macaca mulatta when tested against rabbit anti-human-PF-4. Such immunoglobulin was used for quantitative precipitation of in vivo labelled PF-4 in monkey serum. The results suggest that the active protein had an intra-platelet half-life of about 21 hours. In vitro 125I-labelled human PF-4 was injected intravenously into two monkeys and isolated by immuno-precipita-tion from platelet-poor plasma and from platelets disrupted after gel-filtration. Plasma PF-4 was found to have a half-life of 7 to 11 hours. Some of the labelled PF-4 was associated with platelets and this fraction had a rapid initial disappearance rate and a subsequent half-life close to that of plasma PF-4. The results are compatible with the hypothesis that granular PF-4 belongs to a separate compartment, whereas membrane-bound PF-4 and plasma PF-4 may interchange.

Low Molecular Weight Trypsin-Plasmin Inhibitors Isolated from Papain Treated Urinary Trypsin Inhibitor

1982 ◽  
Vol 47 (01) ◽  
pp. 014-018 ◽  
Author(s):  
H Sumi ◽  
N Toki ◽  
S Takasugi ◽  
S Maehara ◽  
M Maruyama ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Chromatography ◽  
Urinary Trypsin Inhibitor ◽  
Plasmin Activity ◽  
Molecular Weights ◽  
Plasmin Inhibitors

SummaryPapain treatment of human urinary trypsin inhibitor (UTI67; mol. wt. 43,000 by SDS-polyacrylamide gel electrophoresis, specific activity 1,897 U/mg protein) produced four new protease inhibitors, which were highly purified by gel chromatography on Sephadex G-100 and isoelectric focusing. The purified inhibitors (UTI26, UTI9-I, UTI9-II, and UTI9-III) were shown to be homogeneous by polyacrylamide disc gel electrophoresis, and had apparent molecular weights of 26,000, 9,000, 9,000, and 9,800, respectively, by sodium dodecyl sulfate gel electrophoresis. During enzymatic degradation of UTI67, the amino acid compositions changed to more basic, and the isoelectric point increased from pH 2.0 (UTI67) to pHs 4.4, 5.2, 6.6, and 8.3 (UTI26, UTI9-I, UTI9-II, and UTI9-III), respectively. Both the parent and degraded inhibitors had anti-plasmin activity as well as antitrypsin and anti-chymotrypsin activities. Much higher anti-plasmin/anti-trypsin and anti-plasmin/anti-chymotrypsin activities were observed in the degraded inhibitors than in the parent UTI67. They competitively inhibited human plasmin with Ki values of 1.13 X 10-7 - 2.12 X 10-6 M (H-D-Val-Leu-Lys-pNA substrate). The reactions were very fast and the active site of the inhibitors to plasmin was thought to be different from that to trypsin or chymotrypsin.

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