Regulating inhibitory activity of potato I‐type proteinase inhibitor from buckwheat by rutin and quercetin

2021 ◽  
Author(s):  
Xiaodong Cui ◽  
Yifan Lv ◽  
Zhuanhua Wang ◽  
Jiao Li ◽  
Chen Li
Keyword(s):  
Inhibitory Activity ◽  
Proteinase Inhibitor ◽  
Rutin And Quercetin

Rapid screening for deficiency of alpha 1-proteinase inhibitor.

1989 ◽  
Vol 35 (9) ◽  
pp. 1971-1975 ◽  
Author(s):  
C Lloyd ◽  
J Travis
Keyword(s):  
Human Plasma ◽  
Inhibitory Activity ◽  
Proteinase Inhibitor ◽  
Rapid Screening ◽  
Early Screening ◽  
Pancreatic Elastase ◽  
Low Concentrations ◽  
Normal Individuals ◽  
Porcine Pancreatic Elastase ◽  
Alpha 1 Antitrypsin

Abstract This rapid screening procedure for detection of low but functional elastase-inhibitory activity in human plasma is based on the fact that incubation of excess porcine pancreatic elastase (EC 3.4.21.36) with plasma results in formation of a complex with active alpha 1-proteinase inhibitor (alpha 1PI, also called alpha 1-antitrypsin). In normal individuals all of the elastase is complexed, leaving no free enzyme to hydrolyze the elastase substrate, and the reaction mixture remains clear. Because individuals homozygous for the Z allele have relatively low concentrations of alpha 1PI, their plasma cannot complex all of the elastase in the assay. The uncomplexed enzyme hydrolyzes the elastase-specific p-nitroanilide substrate, producing a yellow reaction mixture. Use of this simple assay for early screening of individuals for alpha 1PI deficiency may substantially decrease the number of untreated cases of familial emphysema, a disorder that develops as a result of a genetically derived proteinase-proteinase inhibitor imbalance.

scholarly journals Зміна протеїназно-інгібіторної системи організму здорових білих мишей під дією поляризованого, некогерентного, поліхроматичного світла

2017 ◽  
Author(s):  
N. А. Mamedaliev ◽  
V. A. Divocha ◽  
A. I. Gozhenko
Keyword(s):  
Inhibitory Activity ◽  
Proteinase Inhibitor ◽  
Gamma Globulin ◽  
Antiviral Effect ◽  
Complete Disappearance ◽  
Immune Stimulation ◽  
Inhibitory System ◽  
Experimental Animals ◽  
Epidemic Period ◽  
Healthy Body

Introduction. Along with specific flu prevention, using vaccines other ways do not lose relevance to prevent influenza and SARS, which are non-specific and folk medicines, especially their use in pre-epidemic period. But unspecific methods are related to immune stimulation and focused on antiviral effect. These include stimulants interferon, gamma globulin, Arbidol, Laferon and polarized, polychromatic, incoherent (Payler) light.The aim of the study – to learn enzyme-inhibitory system in a healthy body of white mice and its amendments arising under Payler light.Research Methods. Trypsyn-like proteinase activity was determined by the method of K. I. Veremeienko modified by S. V. Vovchuk. Protein was determined by the method of O. Lowry. Definition proteinase trypsyn-like inhibitor was performed by A. P. Levytskyi.Results and Discussion. As the results of studies in lungs of mice healthy active proteinase inhibitor trypsyn-like lung was 1.16 mg/ml, and serum – 168.7 mg/ml. Proteinases activity in the lungs of mice was 66.4 mg of arginine in 0.1 ml/1 hr; in serum of healthy mice – 51.5 micrograms in 0.1 ml/1 hr. The protein content in the lungs of mice at 6.28 mg/ml in serum of mice – 13.77 mg/ml. In mice that received 11 sessions of exposure Payler-light inhibitory activity in lungs was not determined and in blood serum was recorded at 80.12 mg/ml, under Payler light inhibitory activity decreased by 50 % in serum and completely disappeared in the lungs of experimental animals. Proteinases activity increased to 86.0 mc arg/0.1ml/1 hr. in serum of mice it was 26.7 mg arg/0.1ml/1 hr. The content of total protein in serum blood and lungs of mice was significantly reduced.Conclusions. Under the influence of light-Payler proteinases we observed an increase in activity in the lungs of mice, and protein in the serum. Activity reducing of inhibitor on 50 % was noted in the serum of mice. At the same time, in lungs of animals we observed its complete disappearance.

Human Cystatin A Is Inactivated by Engineered Truncation. The NH2-Terminal Region of the Cysteine Proteinase Inhibitor Is Essential for Expression of Its Inhibitory Activity

Biochemistry ◽  
1995 ◽  
Vol 34 (38) ◽  
pp. 12185-12192 ◽  
Author(s):  
Kazunori Shibuya ◽  
Hiroyuki Kaji ◽  
Takehito Itoh ◽  
Yukihito Ohyama ◽  
Akiyoshi Tsujikami ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Terminal Region ◽  
Cysteine Proteinase Inhibitor ◽  
Cystatin A ◽  
Human Cystatin

scholarly journals Modification of the tandem reactive centres of human inter-α-trypsin inhibitor with butanedione and cis-dichlorodiammineplatinum(II)

1988 ◽  
Vol 254 (1) ◽  
pp. 171-178 ◽  
Author(s):  
M W Swaim ◽  
S V Pizzo
Keyword(s):  
Trypsin Inhibitor ◽  
Inhibitory Activity ◽  
Proteinase Inhibitor ◽  
Complete Loss ◽  
Cathepsin G ◽  
Partial Loss ◽  
Inhibitory Specificity ◽  
Region Sequence ◽  
Leucocyte Elastase ◽  
Kunitz Type

Human inter-alpha-trypsin inhibitor (I alpha I) is a plasma proteinase inhibitor active against cathepsin G, leucocyte elastase, trypsin and chymotrypsin. It owes its broad inhibitory specificity to tandem Kunitz-type inhibitory domains within an N-terminal region. Sequence studies suggest that the reactive-centre residues critical for inhibition are methionine and arginine. Reaction of I alpha I with the arginine-modifying reagent butane-2,3-dione afforded partial loss of inhibitory activity against both cathepsin G and elastase but complete loss of activity against trypsin and chymotrypsin. Reaction of I alpha I with the methionine-modifying reagent cis-dichlorodiammineplatinum(II) resulted in partial loss of activity against cathepsin G and elastase but did not affect inhibition of either trypsin or chymotrypsin. Employment of both reagents eliminated inhibition of cathepsin G and elastase. These findings suggest that both cathepsin G and elastase are inhibited at either of the reactive centres of I alpha I. Trypsin and chymotrypsin, however, appear to be inhibited exclusively at the arginine reactive centre.

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