Human Casein and its Caseino-glycopeptide

WHEN rennin is allowed to react with caseins prepared from milk of different ruminant species at neutral p H and in the presence of calcium, paracasein precipitates and the supernatant contains a glycopeptide, called caseino-glycopeptide 1 : it does not dialyse, and remains soluble in 12 per cent tr...

Full description

Saved in:
Bibliographic Details
Published in:Nature (London) 1962-12, Vol.196 (4859), p.1098-1099
Main Authors: ALAIS, CHARLES, JOLLÈS, PIERRE
Format: Article
Language:English
Subjects:
Caseins
Glycopeptides
Humanities and Social Sciences
Humans
letter
multidisciplinary
Old Medline
Peptides
Science
Science (multidisciplinary)
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c342t-f637107cf1c4575301955bc9090f3a245b163f7de39a699d1b708b3158aec353
cites cdi_FETCH-LOGICAL-c342t-f637107cf1c4575301955bc9090f3a245b163f7de39a699d1b708b3158aec353
container_end_page 1099
container_issue 4859
container_start_page 1098
container_title Nature (London)
container_volume 196
creator ALAIS, CHARLES
JOLLÈS, PIERRE
description WHEN rennin is allowed to react with caseins prepared from milk of different ruminant species at neutral p H and in the presence of calcium, paracasein precipitates and the supernatant contains a glycopeptide, called caseino-glycopeptide 1 : it does not dialyse, and remains soluble in 12 per cent tri-chloroacetic acid (TCA). We prepared and analysed recently the caseino-glycopeptides from cow, goat and sheep caseins, which are analogous but not identical substances 1 . In the case of cow's casein the glycopeptide was obtained from χ-casein by rennin digestion in the absence of calcium 1 . χ-casein has been analysed 2 and seems to be the specific substrate for rennin. In this paper we want to report the amino-acid composition of human casein and to comment on some results concerning its digestion by rennin.
doi_str_mv 10.1038/1961098a0
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_83140769</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>83140769</sourcerecordid><originalsourceid>FETCH-LOGICAL-c342t-f637107cf1c4575301955bc9090f3a245b163f7de39a699d1b708b3158aec353</originalsourceid><addsrcrecordid>eNpt0E1Lw0AQBuBFFFurB_-A9iRUiM50s19HCWqFgpfew2azKSnJJu4mh_57IwntxdMy7MPLzEvIPcILApWvqDiCkhouyBxjwaOYS3FJ5gBrGYGkfEZuQjgAAEMRX5MZxoDIUc7JatPX2i0THWzpltrly7IL09hE--pomta2XZnbW3JV6CrYu-ldkN3H-y7ZRNvvz6_kbRsZGq-7qOBUIAhToImZYBRQMZYZBQoKqtcxy5DTQuSWKs2VyjETIDOKTGprKKML8jTGtr756W3o0roMxlaVdrbpQyrpsLzgaoCrERrfhOBtkba-rLU_pgjpXy3pqZbBPkyhfVbb_CynHgbwPIIwfLm99emh6b0b7vw37XHETne9t-e0k_gF9p1xwQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>83140769</pqid></control><display><type>article</type><title>Human Casein and its Caseino-glycopeptide</title><source>Nature</source><creator>ALAIS, CHARLES ; JOLLÈS, PIERRE</creator><creatorcontrib>ALAIS, CHARLES ; JOLLÈS, PIERRE</creatorcontrib><description>WHEN rennin is allowed to react with caseins prepared from milk of different ruminant species at neutral p H and in the presence of calcium, paracasein precipitates and the supernatant contains a glycopeptide, called caseino-glycopeptide 1 : it does not dialyse, and remains soluble in 12 per cent tri-chloroacetic acid (TCA). We prepared and analysed recently the caseino-glycopeptides from cow, goat and sheep caseins, which are analogous but not identical substances 1 . In the case of cow's casein the glycopeptide was obtained from χ-casein by rennin digestion in the absence of calcium 1 . χ-casein has been analysed 2 and seems to be the specific substrate for rennin. In this paper we want to report the amino-acid composition of human casein and to comment on some results concerning its digestion by rennin.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/1961098a0</identifier><identifier>PMID: 14011618</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Caseins ; Glycopeptides ; Humanities and Social Sciences ; Humans ; letter ; multidisciplinary ; Old Medline ; Peptides ; Science ; Science (multidisciplinary)</subject><ispartof>Nature (London), 1962-12, Vol.196 (4859), p.1098-1099</ispartof><rights>Springer Nature Limited 1962</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c342t-f637107cf1c4575301955bc9090f3a245b163f7de39a699d1b708b3158aec353</citedby><cites>FETCH-LOGICAL-c342t-f637107cf1c4575301955bc9090f3a245b163f7de39a699d1b708b3158aec353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2726,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14011618$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ALAIS, CHARLES</creatorcontrib><creatorcontrib>JOLLÈS, PIERRE</creatorcontrib><title>Human Casein and its Caseino-glycopeptide</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>WHEN rennin is allowed to react with caseins prepared from milk of different ruminant species at neutral p H and in the presence of calcium, paracasein precipitates and the supernatant contains a glycopeptide, called caseino-glycopeptide 1 : it does not dialyse, and remains soluble in 12 per cent tri-chloroacetic acid (TCA). We prepared and analysed recently the caseino-glycopeptides from cow, goat and sheep caseins, which are analogous but not identical substances 1 . In the case of cow's casein the glycopeptide was obtained from χ-casein by rennin digestion in the absence of calcium 1 . χ-casein has been analysed 2 and seems to be the specific substrate for rennin. In this paper we want to report the amino-acid composition of human casein and to comment on some results concerning its digestion by rennin.</description><subject>Caseins</subject><subject>Glycopeptides</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>letter</subject><subject>multidisciplinary</subject><subject>Old Medline</subject><subject>Peptides</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1962</creationdate><recordtype>article</recordtype><recordid>eNpt0E1Lw0AQBuBFFFurB_-A9iRUiM50s19HCWqFgpfew2azKSnJJu4mh_57IwntxdMy7MPLzEvIPcILApWvqDiCkhouyBxjwaOYS3FJ5gBrGYGkfEZuQjgAAEMRX5MZxoDIUc7JatPX2i0THWzpltrly7IL09hE--pomta2XZnbW3JV6CrYu-ldkN3H-y7ZRNvvz6_kbRsZGq-7qOBUIAhToImZYBRQMZYZBQoKqtcxy5DTQuSWKs2VyjETIDOKTGprKKML8jTGtr756W3o0roMxlaVdrbpQyrpsLzgaoCrERrfhOBtkba-rLU_pgjpXy3pqZbBPkyhfVbb_CynHgbwPIIwfLm99emh6b0b7vw37XHETne9t-e0k_gF9p1xwQ</recordid><startdate>19621215</startdate><enddate>19621215</enddate><creator>ALAIS, CHARLES</creator><creator>JOLLÈS, PIERRE</creator><general>Nature Publishing Group UK</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19621215</creationdate><title>Human Casein and its Caseino-glycopeptide</title><author>ALAIS, CHARLES ; JOLLÈS, PIERRE</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c342t-f637107cf1c4575301955bc9090f3a245b163f7de39a699d1b708b3158aec353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1962</creationdate><topic>Caseins</topic><topic>Glycopeptides</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>letter</topic><topic>multidisciplinary</topic><topic>Old Medline</topic><topic>Peptides</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ALAIS, CHARLES</creatorcontrib><creatorcontrib>JOLLÈS, PIERRE</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ALAIS, CHARLES</au><au>JOLLÈS, PIERRE</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Casein and its Caseino-glycopeptide</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1962-12-15</date><risdate>1962</risdate><volume>196</volume><issue>4859</issue><spage>1098</spage><epage>1099</epage><pages>1098-1099</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><abstract>WHEN rennin is allowed to react with caseins prepared from milk of different ruminant species at neutral p H and in the presence of calcium, paracasein precipitates and the supernatant contains a glycopeptide, called caseino-glycopeptide 1 : it does not dialyse, and remains soluble in 12 per cent tri-chloroacetic acid (TCA). We prepared and analysed recently the caseino-glycopeptides from cow, goat and sheep caseins, which are analogous but not identical substances 1 . In the case of cow's casein the glycopeptide was obtained from χ-casein by rennin digestion in the absence of calcium 1 . χ-casein has been analysed 2 and seems to be the specific substrate for rennin. In this paper we want to report the amino-acid composition of human casein and to comment on some results concerning its digestion by rennin.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>14011618</pmid><doi>10.1038/1961098a0</doi><tpages>2</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0028-0836
ispartof Nature (London), 1962-12, Vol.196 (4859), p.1098-1099
issn 0028-0836
1476-4687
language eng
recordid cdi_proquest_miscellaneous_83140769
source Nature
subjects Caseins
Glycopeptides
Humanities and Social Sciences
Humans
letter
multidisciplinary
Old Medline
Peptides
Science
Science (multidisciplinary)
title Human Casein and its Caseino-glycopeptide
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T12%3A56%3A01IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Human%20Casein%20and%20its%20Caseino-glycopeptide&rft.jtitle=Nature%20(London)&rft.au=ALAIS,%20CHARLES&rft.date=1962-12-15&rft.volume=196&rft.issue=4859&rft.spage=1098&rft.epage=1099&rft.pages=1098-1099&rft.issn=0028-0836&rft.eissn=1476-4687&rft_id=info:doi/10.1038/1961098a0&rft_dat=%3Cproquest_cross%3E83140769%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c342t-f637107cf1c4575301955bc9090f3a245b163f7de39a699d1b708b3158aec353%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=83140769&rft_id=info:pmid/14011618&rfr_iscdi=true