scholarly journals Isolation and properties of multiple forms of histidine decarboxylase from rat gastric mucosa

1982 ◽  
Vol 205 (2) ◽  
pp. 405-412 ◽  
Author(s):  
A Savany ◽  
L Cronenberger
Keyword(s):  
Gastric Mucosa ◽  
Isoelectric Focusing ◽  
Histidine Decarboxylase ◽  
Specific Activity ◽  
Proteinase Inhibitors ◽  
Gel Chromatography ◽  
High Loss ◽  
Carrier Ampholytes ◽  
Km Value ◽  
Rat Gastric Mucosa

The heterogeneity of histidine decarboxylase from rat gastric mucosa was studied. The partially purified enzyme was fractionated by preparative isoelectric focusing on a flat-gel bed by using narrow pH-range carrier ampholytes and a short focusing time. The activity was resolved, with about 95% recovery, into three forms, designated I, II and III, with pI values of 5.90, 5.60 and 5.35 respectively. These three forms exhibited similar molecular weights, indicating that the forms were not the result of different degrees of polymerization. By preparative refocusing each form refocused as a single peak of enzyme activity with reproducible pI, but a high loss of activity occurred with repeated focusing. Forms I, II and III were purified by the combined use of preparative isoelectric focusing and gel chromatography and other fractionation methods. The active forms could be distinguished by electrophoresis and isoelectric focusing on polyacrylamide gels and displayed protein heterogeneity. These forms were found in the crude extract and in the partially purified preparations in the presence or absence of proteinase inhibitors. Form II had the highest specific activity, but all three forms had the same optimum pH and Km value for histidine.

scholarly journals Electron microscopic identification of histidine decarboxylase-containing endocrine cells of the rat gastric mucosa

1984 ◽  
Vol 87 (3) ◽  
pp. 496-502 ◽  
Author(s):  
Hiroaki Kubota ◽  
Yoshitaka Taguchi ◽  
Masaya Tohyama ◽  
Nariaki Matsuura ◽  
Sadao Shiosaka ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Endocrine Cells ◽  
Histidine Decarboxylase ◽  
Electron Microscopic ◽  
Microscopic Identification ◽  
Rat Gastric Mucosa ◽  
Electron Microscopic Identification

Water Extracts of Helicobacter pylori Suppress the Expression of Histidine Decarboxylase and Reduce Histamine Content in the Rat Gastric Mucosa

Digestion ◽  
2000 ◽  
Vol 62 (2-3) ◽  
pp. 100-109 ◽  
Author(s):  
Peter C. Konturek ◽  
Tomasz Brzozowski ◽  
Elżbieta Karczewska ◽  
Aleksandra Duda ◽  
Władysław Bielański ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Gastric Mucosa ◽  
Histidine Decarboxylase ◽  
Histamine Content ◽  
Water Extracts ◽  
Rat Gastric Mucosa

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.

Sign in / Sign up

Export Citation Format

Share Document