Evidence map›Paper›PMID 31271254›Full record

ArticleMolecular nutrition & food research2019

Selective Proteolysis of α-Lactalbumin by Endogenous Enzymes of Human Milk at Acidic pH.

Junai Gan, Jingyuan Zheng, Nithya Krishnakumar, Elisha Goonatilleke, Carlito B Lebrilla, Daniela Barile, J Bruce German

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular nutrition & food research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. 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 at 1 institution in 1 country.

Junai GanDepartment of Food Science and Technology, University of California, Davis, CA, 95616, USA.ORCID 0000-0002-8326-5375
Jingyuan ZhengDepartment of Nutrition, University of California, Davis, CA, 95616, USA.
Nithya KrishnakumarDepartment of Food Science and Technology, University of California, Davis, CA, 95616, USA.
Elisha GoonatillekeDepartment of Chemistry, University of California, Davis, CA, 95616, USA.
Carlito B LebrillaDepartment of Chemistry, University of California, Davis, CA, 95616, USA.
Daniela BarileDepartment of Food Science and Technology, University of California, Davis, CA, 95616, USA.
J Bruce GermanDepartment of Food Science and Technology, University of California, Davis, CA, 95616, USA.
University of California, Davis · US

Funding

Activation of probiotic bifidobacteria by milk glyansR01AT008759 · NCCIH · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GERMAN, BRUCE, LEBRILLA, CARLITO B · 2014 to 2018
$4.2M
Mechanism of Activation of Probiotic Bifidobacteria by Prebiotic Milk GlycansR01AT007079 · NCCIH · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GERMAN, BRUCE, LEBRILLA, CARLITO B · 2012 to 2016
$2.2M
NCCIH NIH HHS R01 AT007079NCCIH NIH HHS R01 AT008759
6 · The paper itself

Abstract

scopeThe use of human milk products is increasing for high-risk infants. Human milk contains endogenous enzymes that comprise a dynamic proteolytic system, yet biological properties of these enzymes and their activities in response to variations including pH within infants are unclear. Human milk has a neutral pH around 7, while infant gastric pH varies from 2 to 6 depending on individual conditions. This study is designed to determine the specificity of enzyme-substrate interactions in human milk as a function of pH. METHODS AND

resultsEndogenous proteolysis is characterized by incubating freshly expressed human milk at physiologically relevant pH ranging from 2 to 7 without the addition of exogenous enzymes. Results show that the effects of pH on endogenous proteolysis in human milk are protein-specific. Further, specific interactions between cathepsin D and α-lactalbumin are confirmed. The endogenous enzyme cathepsin D in human milk cleaves α-lactalbumin as the milk pH shifts from 7 to 3.

conclusionsThis study documents that selective proteolysis activated by pH shift is a mechanism for dynamic interactions between human milk and the infant. Controlled proteolysis can guide the use of human milk products based on individual circumstance.

Indexed as

Cathepsin DChromatography, LiquidHumansHydrogen-Ion ConcentrationLactalbuminMilk, HumanMilk ProteinsProteolysisSubstrate SpecificityTandem Mass SpectrometryCathepsin DLactalbuminMilk Proteinsbioactivityhuman milkpHproteinselective proteolysis

Identifiers

PMID31271254
PMCPMC7231428
OpenAlexW2954566975

What OpenQuestion holds

Textmetadata
LicenceTDM
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.