Evidence map›Paper›PMID 24595088›Full record

ArticlePloS one2014

Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin.

Nilisha Rastogi, Nitish Nagpal, Hammad Alam, Sadanand Pandey, Lovely Gautam, Mau Sinha, Kouichirou Shin, Nikhat Manzoor, Jugsharan S Virdi, Punit Kaur and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Proteolysis of vaginally administered bovine lactoferrin: clearance, inter-subject variability, and implications for clinical dosing.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
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

12 authors at 4 institutions in 2 countries.

Nilisha RastogiDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
Nitish NagpalDepartment of Microbiology, University of Delhi, South Campus, New Delhi, India.
Hammad AlamDepartment of Biosciences, Jamia Milia Islamia, New Delhi, India.
Sadanand PandeyDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
Lovely GautamDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
Mau SinhaDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
Kouichirou ShinFood Science & Technology Institute, Morinaga Milk Industry Co. Ltd., Zama, Kanagawa, Japan.
Nikhat ManzoorDepartment of Biosciences, Jamia Milia Islamia, New Delhi, India.
Jugsharan S VirdiDepartment of Microbiology, University of Delhi, South Campus, New Delhi, India.
Punit KaurDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
Sujata SharmaDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
Tej P SinghDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
All India Institute of Medical Sciences · INJamia Millia Islamia · INUniversity of Delhi · INMegmilk Snow Brand (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactoferrin is an 80 kDa bilobal, iron binding glycoprotein which is primarily antimicrobial in nature. The hydrolysis of lactoferrin by various proteases in the gut produces several functional fragments of lactoferrin which have varying molecular sizes and properties. Here, bovine lactoferrin has been hydrolyzed by trypsin, the major enzyme present in the gut, to produce three functional molecules of sizes approximately 21 kDa, 38 kDa and 45 kDa. The molecules have been purified using ion exchange and gel filtration chromatography and identified using N-terminal sequencing, which reveals that while the 21 kDa molecule corresponds to the N2 domain (21LF), the 38 kDa represents the whole C-lobe (38LF) and the 45 kDa is a portion of N1 domain of N-lobe attached to the C-lobe (45LF). The iron binding and release properties of 21LF, 38LF and 45LF have been studied and compared. The sequence and structure analysis of the portions of the excision sites of LF from various species have been done. The antibacterial properties of these three molecules against bacterial strains, Streptococcus pyogenes, Escherichia coli, Yersinia enterocolitica and Listeria monocytogenes were investigated. The antifungal action of the molecules was also evaluated against Candida albicans. This is the first report on the antimicrobial actions of the trypsin cleaved functional molecules of lactoferrin from any species.

Indexed as

Amino Acid SequenceAnimalsAnti-Infective AgentsCattleChromatography, Ion ExchangeHydrogen-Ion ConcentrationLactoferrinModels, MolecularMolecular Sequence DataPeptide FragmentsPeptide MappingSequence Homology, Amino AcidTrypsinAnti-Infective AgentsLactoferrinPeptide FragmentsTrypsin

Identifiers

PMID24595088
PMCPMC3940724
OpenAlexW1973610993

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.