Virgie G. Shore

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTHeterogeneity of human plasma very low density lipoproteins. Separation of species differing in protein componentsVirgie G. Shore and Bernard ShoreCite this: Biochemistry 1973, 12, 3, 502–507Publication Date (Print):January 1, 1973Publication History Published online1 May 2002Published inissue 1 January 1973https://pubs.acs.org/doi/10.1021/bi00727a022https://doi.org/10.1021/bi00727a022research-articleACS PublicationsRequest reuse permissionsArticle Views441Altmetric-Citations259LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTCofactor activity of protein components of human very low density lipoproteins in the hydrolysis of triglycerides by lipoprotein lipase from different sourcesRichard J. Havel, Christopher J. Fielding, Thomas Olivecrona, Virgie G. Shore, Phoebe E. Fielding, and Torbjorn EgelrudCite this: Biochemistry 1973, 12, 9, 1828–1833Publication Date (Print):April 24, 1973Publication History Published online1 May 2002Published inissue 24 April 1973https://pubs.acs.org/doi/10.1021/bi00733a026https://doi.org/10.1021/bi00733a026research-articleACS PublicationsRequest reuse permissionsArticle Views305Altmetric-Citations258LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

Lipoprotein lipase forms an enzyme-substrate complex with fat emulsions in the presence of serum lipoproteins. Lipoproteins of very low density and high density have this property, but the former are much more active per unit weight of protein. In this investigation, the activity, expressed as quantity giving half-maximal rate of production of free fatty acids, of specific glycopeptides isolated from very low density and high density lipoproteins was tested in an incubation mixture containing lipoprotein lipase from cows' milk and 1.8 mg triglyceride per ml. The two major polypeptides of high density lipoproteins were virtually inactive in amounts up to 100 µg per ml. Activity of the unfractionated apoproteins of very low density lipoprotein was similar to that of the native lipoprotein (about 4 µg/ml). Two of its polypeptides were active: one with carboxyl-terminal glutamic acid at 0.45 to 0.60µg/ml and one with carboxyl-terminal alanine at 1.8.2.8 µg/ml. Some preparations of the latter peptide were less active and inhibited at high levels. Three other glycopeptides from very low density lipoprotein were inactive. Low density lipoprotein from subjects with primary biliary cirrhosis and a lipoprotein of density 1.04 to 1.06 from a subject with specific elevation of this fraction, both containing the active glycopeptides, had considerable activity (5 to 11 µg/ml). These studies indicate that specific glycopeptides are required for the action of lipoprotein lipase on emulsified triglycerides and suggest that they are important components of the mechanism for extra-hepatic utilization of plasma triglycerides.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTIsolation and characterization of polypeptides of human serum lipoproteinsBernard Shore and Virgie G. ShoreCite this: Biochemistry 1969, 8, 11, 4510–4516Publication Date (Print):November 1, 1969Publication History Published online1 May 2002Published inissue 1 November 1969https://pubs.acs.org/doi/10.1021/bi00839a043https://doi.org/10.1021/bi00839a043research-articleACS PublicationsRequest reuse permissionsArticle Views95Altmetric-Citations203LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts