Evidence map›Paper›PMID 28662655›Full record

ArticleBMC veterinary research2017

Identification, characterization and purification of porcine Quiescin Q6-Sulfydryl Oxidase 2 protein.

Yu-Wen Kuo, Radhika Joshi, Tse-En Wang, Hui-Wen Chang, Sheng-Hsiang Li, Chun-Ni Hsiao, Pei-Shiue Jason Tsai

Open access · goldAbstract read
In one paragraph

Article in BMC veterinary research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Proteomic and functional analysis of alpaca (Frontiers in veterinary science · 2025
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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 at 2 institutions in 1 country.

Yu-Wen KuoDepartment of Veterinary Medicine, National Taiwan University, No. 1, Sec. 4, Roosevelt Rd, 10617, Taipei, Taiwan.
Radhika JoshiDepartment of Veterinary Medicine, National Taiwan University, No. 1, Sec. 4, Roosevelt Rd, 10617, Taipei, Taiwan.
Tse-En WangDepartment of Veterinary Medicine, National Taiwan University, No. 1, Sec. 4, Roosevelt Rd, 10617, Taipei, Taiwan.
Hui-Wen ChangDepartment of Veterinary Medicine, National Taiwan University, No. 1, Sec. 4, Roosevelt Rd, 10617, Taipei, Taiwan.
Sheng-Hsiang LiDepartment of Medical Research, Mackay Memorial Hospital, No. 92, Section 2, Zhongshan N. Rd, 251 Tamshui, Taipei, Taiwan.
Chun-Ni HsiaoDepartment of Veterinary Medicine, National Taiwan University, No. 1, Sec. 4, Roosevelt Rd, 10617, Taipei, Taiwan.
Pei-Shiue Jason TsaiDepartment of Veterinary Medicine, National Taiwan University, No. 1, Sec. 4, Roosevelt Rd, 10617, Taipei, Taiwan. psjasontsai@ntu.edu.tw.
National Taiwan University · TWMackay Memorial Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPost-spermiogenesis membrane surface modifications rely on molecules present in the reproductive tracts. Two isoforms (isoform 1 and 2) from Quiescin Q6-Sulfydryl Oxidase protein family have been identified in the male reproductive tract of rodent species. However, unlike isoform 1, scarce information is available for isoform 2, likely due to its lower expression level and lack of proper purification methods to obtain sufficient protein quantity for further assays.

resultsThis study demonstrated the presence of short and long forms of Quiescin Q6-Sulfydryl Oxidase 2 in boar, likely representing the secretory (short form) and transmembrane (long form) forms of Quiescin Q6-Sulfydryl Oxidase 2. Immunohistochemistry studies revealed the presence of Quiescin Q6-Sulfydryl Oxidase 2 in a broad range of porcine tissues; the pronounced vesicle-contained Quiescin Q6-Sulfydryl Oxidase 2 at the apical region of epididymis and seminal vesicles epithelium suggested its involvement in sperm physiology and its participation in semen formation. The majority of porcine Quiescin Q6-Sulfydryl Oxidase 2 could be purified via either antibody affinity column or be salted out using 10%-40% ammonium sulfate. Higher amount of low molecular weight Quiescin Q6-Sulfydryl Oxidase 2 observed in the seminal vesicle likely represents the secretory form of Quiescin Q6-Sulfydryl Oxidase 2 and reflects an exuberant secretory activity in this organ.

conclusionsWe demonstrated for the first time, the presence of Quiescin Q6-Sulfydryl Oxidase 2 in porcine species; moreover, two forms of Quiescin Q6-Sulfydryl Oxidase 2 were identified and exhibited distinct molecular weights and properties during protein purification processes. This study also provided feasible Quiescin Q6-Sulfydryl Oxidase 2 purification methods from slaughterhouse materials that could potentially allow obtaining sufficient amount of Quiescin Q6-Sulfydryl Oxidase 2 for future functional investigations.

Indexed as

AnimalsEpididymisImmunohistochemistryMaleMice, Inbred ICROxidoreductasesOxidoreductases Acting on Sulfur Group DonorsSeminal VesiclesSwineOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsEpididymisPorcineQuiescin Q6-Sulfydryl OxidaseSeminal vesicle

Identifiers

PMID28662655
PMCPMC5492681
OpenAlexW2733604669

What OpenQuestion holds

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LicenceCC BY
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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.