Evidence map›Paper›PMID 38924451›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2024

Chromatographic purification of the plasmin-like enzyme from clamworm (Perinereis aibuhitensis Grub) and its fibrinolytic activity by metal ions.

Tuo Song, Xinyuan Han, Tingting Jiang, Xinyi Pu, Mingjun Wei, Yuping Zhu, Wenhui Wu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2024. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Chromatographic purification of the plasmin-like enzyme from clamworm (Perinereis aibuhitensis Grub) and its fibrinolytic activity by metal ions.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    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

7 authors.

Tuo SongDepartment of Marine Biopharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai, China.ORCID https://orcid.org/0009-0003-0641-0123
Xinyuan HanDepartment of Marine Biopharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Tingting JiangDepartment of Marine Biopharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Xinyi PuDepartment of Marine Biopharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Mingjun WeiDepartment of Marine Biopharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Yuping ZhuDepartment of Clinical Medicine, Naval Medical University, Shanghai, China.
Wenhui WuDepartment of Marine Biopharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai, China.ORCID https://orcid.org/0000-0002-1710-8582

Funding

MOST | National Natural Science Foundation of China (NSFC) 82173731Research fund of international Young Scientist 81750110548Shanghai Frontiers Research Center of the Hadal Biosphere
6 · The paper itself

Abstract

In this study, fibrinolytic protease was isolated and purified from Perinereis aibuhitensis Grub, and the extraction process was optimized. The properties of the enzyme, such as the amino acid composition, thermal stability, optimal temperature, and pH, were investigated. After detoxification, proteins collected from fresh Clamworm (Perinereis aibuhitensis Grub) were concentrated via ammonium sulfate precipitation. The crude protease was purified using gel filtration resin (Sephadex G-100), anion exchange resin (DEAE-Sepharose FF), and hydrophobic resin (Phenyl Sepharose 6FF). The molecular weight of the protease was determined by polyacrylamide gel electrophoresis (SDS-PAGE). The optimum temperature and optimum pH of the protease were determined. The activity of crude protease in the 40-60% salt-out section was the highest, reaching 467.53 U/mg. The optimal process for purifying crude protein involved the application of DEAE-Sepharose FF and Phenyl Sepharose 6FF, which resulted in the isolation of a single protease known as Asp60-D1-P1 with the highest fibrinolytic activity; additionally, the enzyme activity was measured at 3367.76 U/mg. Analysis by Native-PAGE and SDS-PAGE revealed that the molecular weight of Asp60-D1-P1 was 44.5 kDa, which consisted of two subunits with molecular weights of 6.5 and 37.8 kDa, respectively. The optimum temperature for Asp60-D1-P1 was 40°C, and the optimal pH was 8.0.

Indexed as

FibrinolysinAnimalsElectrophoresis, Polyacrylamide GelEnzyme StabilityFibrinolytic AgentsHydrogen-Ion ConcentrationMetalsMolecular WeightPolychaetaTemperatureFibrinolysinFibrinolytic AgentsMetalsfibrinolytic activity measurefibrinolytic proteasePerinereis aibuhitensis Grubprotease purification

Identifiers

PMID38924451
PMCPMC13688079

What OpenQuestion holds

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Registered trials

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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.