Purification and identification of β-casein phosphopeptide (1-25)-Reference-Cited by-同舟云学术

Purification and identification of β-casein phosphopeptide (1-25)

Published:2016-10 Issue:10 Volume:99 Page:7803-7808
ISSN:0022-0302
Container-title:Journal of Dairy Science
language:en
Short-container-title:Journal of Dairy Science

Author:

Naqvi Muhammad Ali,Singh Jasjit,Han Eugene,Farshad Koushan,Rousseau Dérick

Funder

Natural Sciences and Engineering Research Council of Canada

Dairy Farmers of Canada

Ryerson University

Advanced Foods and Materials Network

Publisher

American Dairy Science Association

Subject

Genetics,Animal Science and Zoology,Food Science

Reference19 articles.

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3. Phosphorylation and coordination bond of mineral inhibit the hydrolysis of the beta-casein (1–25) peptide by intestinal brush-border membrane enzymes;Boutrou;J. Agric. Food Chem.,2010

4. Identification of protein phosphorylation sites by a combination of mass spectrometry and solid phase Edman sequencing;Campbell;J. Biomol. Tech.,2002

5. Calcium ions enclosed in casein phosphopeptide aggregates are directly involved in the mineral uptake by differentiated HT-29 cells;Cosentino;Int. Dairy J.,2010

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2. A comprehensive review on preparation, structure-activities relationship, and calcium bioavailability of casein phosphopeptides;Critical Reviews in Food Science and Nutrition;2022-09-02

3. Clinical relevance to the physicochemical properties of allergen molecules;Nihon Shoni Arerugi Gakkaishi. The Japanese Journal of Pediatric Allergy and Clinical Immunology;2020-03-20

4. The purification, identification and bioactivity study of a novel calcium-binding peptide from casein hydrolysate;Food & Function;2019