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In-vitro anti-inflammatory activity of serine protease inhibitor from Cassia siamea and Dolichos biflorus: A comparative study.

التفاصيل البيبلوغرافية
العنوان: In-vitro anti-inflammatory activity of serine protease inhibitor from Cassia siamea and Dolichos biflorus: A comparative study.
المؤلفون: Honnenahalli Rajegowda S; Department of Studies and Research in Biochemistry, Jnana Kaveri Post Graduate Centre, Mangalore University, Kodagu, Karnataka, India., Athahalli Honnagirigowda SR; Department of Studies and Research in Biochemistry, Jnana Kaveri Post Graduate Centre, Mangalore University, Kodagu, Karnataka, India.
المصدر: Cell biochemistry and function [Cell Biochem Funct] 2023 Jan; Vol. 41 (1), pp. 33-44. Date of Electronic Publication: 2022 Oct 17.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Wiley-Blackwell Country of Publication: England NLM ID: 8305874 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1099-0844 (Electronic) Linking ISSN: 02636484 NLM ISO Abbreviation: Cell Biochem Funct Subsets: MEDLINE
أسماء مطبوعة: Publication: Oxford, England : Wiley-Blackwell
Original Publication: Guildford, Surrey : Butterworth Scientific Ltd., c1983-
مواضيع طبية MeSH: Dolichos*/chemistry , Dolichos*/metabolism , Cassia*/metabolism, Serine Proteinase Inhibitors/pharmacology ; Trypsin/chemistry ; Trypsin/metabolism ; Enzyme Inhibitors ; Hydrogen-Ion Concentration
مستخلص: Cassia siamea is a nonedible legume belonging to Fabaceae. The seed of C. siamea contains ~16% of protein. The study reports the biochemical characterization of purified novel serine protease inhibitor from seeds of C. siamea, aimed with assessing the anti-inflammatory activity. The seed extract was subjected to ammonium sulfate precipitation followed by fast protein liquid chromatography (FPLC)-anion exchange chromatography and affinity-chromatography to obtain a relative pure protease inhibitor. Thirty-fivefold purification with the specific activity of 250 U/mg of trypsin inhibitory unit was obtained. The characterization of protease inhibitor for optimum temperature, pH, and metal ions were measured using N-α-benzoyl-DL-arginine-p-nitroanilide (BAPNA) assay and casein zymogram. The C. siamea trypsin inhibitor (CsTI) has a relative molecular mass of 25.540 kDa. Purified CsTI and Dolichos biflorus were tested for anti-inflammatory efficacy against A549 and RAW264.7 cell lines. The inhibitory activity of both purified inhibitors are comparable and are potent toward anti-inflammatory activity. The purified inhibitor shows to be a promising candidate as anti-inflammatory agent by targeting the serine proteases.
(© 2022 John Wiley & Sons Ltd.)
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فهرسة مساهمة: Keywords: IL-6; TNF-α; anti-inflammatory; elastase; nitrite; protease inhibitor; reverse casein zymogram
المشرفين على المادة: 0 (Serine Proteinase Inhibitors)
EC 3.4.21.4 (Trypsin)
0 (Enzyme Inhibitors)
تواريخ الأحداث: Date Created: 20221017 Date Completed: 20230110 Latest Revision: 20230111
رمز التحديث: 20231215
DOI: 10.1002/cbf.3758
PMID: 36250219
قاعدة البيانات: MEDLINE
الوصف
تدمد:1099-0844
DOI:10.1002/cbf.3758