Evidence map›Paper›PMID 11195976›Full record

ArticleJournal of protein chemistry2000

Purification and characterization of a trypsin-like enzyme with fibrinolytic activity present in the abdomen of horn fly, Haematobia irritans irritans (Diptera: Muscidae).

M Dametto, A P David, S S Azzolini, I T Campos, A M Tanaka, A Gomes, R Andreotti, A S Tanaka

Abstract read
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Article in Journal of protein chemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.2field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

M DamettoDepartamento de Bioquímica, Universidade Federal de São Paulo, Escola Paulista de Medicina, SP, Brazil.
A P David
S S Azzolini
I T Campos
A M Tanaka
A Gomes
R Andreotti
A S Tanaka
Universidade Federal de São Paulo · BRBrazilian Agricultural Research Corporation · BRInstituto Butantan · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This work describes the purification and characterization of a trypsin-like enzyme with fibrinolytic activity present in the abdomen of Haematobia irritans irritans (Diptera: Muscidae). The enzyme was purified using a one-step process, consisting of affinity chromatography on SBTI-Sepharose. The purified protease showed one major active proteinase band on reverse zymography with 0.15% gelatin, corresponding to a molecular mass of 25.5 kDa, with maximum activity at pH 9.0. The purified trypsin-like enzyme preferentially hydrolyzed synthetic substrates with arginine residue at the P1 position. The Km values determined for three different substrates were 1.88 x 10(-4), 1.28 x 10(-4), and 1.40 x 10(-4) M for H-alpha-benzoyl-Ile-Glu-Gly-Arg-p-nitroanilide (S2222), DL-Ile-Pro-Arg-p-nitroanilide (S2288), and DL-Phe-Pip-Arg-p-nitroanilide (S2238), respectively. The enzyme was strongly inhibited by typical serine proteinase inhibitors such as SB

Indexed as

AnimalsFibrinFibrinolytic AgentsHumansHydrogen-Ion ConcentrationMolecular WeightMuscidaeSerine EndopeptidasesSubstrate SpecificityFibrinFibrinolytic AgentsSerine Endopeptidasestrypsin-like serine protease

Identifiers

PMID11195976
OpenAlexW1575596815

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.