Evidence map›Paper›PMID 40715764›Full record

ArticleCurrent microbiology2025

Purification and Characterization of Non-hemolytic Fibrinolytic Protease From Newly Isolated Proteus penneri SP 20.

Sowmya B Jhample, Prashant K Bhagwat, Nisha A Nerlekar, Vinod S Nandre, Padma B Dandge

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Article in Current microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Sowmya B JhampleDepartment of Biochemistry, Shivaji University, Kolhapur, 416004, M.S., India.
Prashant K BhagwatDepartment of Microbiology, Shivaji University, Kolhapur, 416004, M.S., India.
Nisha A NerlekarDepartment of Biochemistry, Shivaji University, Kolhapur, 416004, M.S., India.
Vinod S NandreDepartment of Chemistry, Division of Biochemistry, Savitribai Phule Pune University, Pune, 411007, M.S., India.
Padma B DandgeDepartment of Biochemistry, Shivaji University, Kolhapur, 416004, M.S., India. pbd_biochem@unishivaji.ac.in.

Funding

UGC-MRP F.No.41-1282/2012 (SR).UGC-RGNF F1-17.1/2013-14/RGNF-2013-14-SC-MAH-51593
6 · The paper itself

Abstract

The most common cause of cardiovascular diseases which impact blood arteries is thrombosis. Current medications and protein-based treatments are examples of thrombolytic agents. Finding new enzymatic sources is essential in health difficulties because all of these agents have unfavorable side effects. By taking this fact into account, this study presents the purification and biochemical characterization of a fibrinolytic metalloprotease from Proteus penneri SP-20 (AB909494) as a new isolate. The enzyme was successfully purified using DEAE-cellulose anion exchange chromatography at a recovery rate of 58.73% and at 33.38 purification fold. The SDS-PAGE examination yielded a molecular mass of 16 kDa. The isolated enzyme was most active at 40 °C and pH 6.0. The purified enzyme maximal velocity (Vmax) and Michaelis constant (Km) were determined to be 6 × 10-4 mol/L/min and 2.07 mg/mL, respectively. Phenanthroline, EDTA, Hg

Indexed as

Bacterial ProteinsFibrinolytic AgentsMetalloproteasesProteusEnzyme StabilityHumansHydrogen-Ion ConcentrationKineticsMolecular WeightTemperatureBacterial ProteinsFibrinolytic AgentsMetalloproteases

Identifiers

PMID40715764

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