Two harvests of ocean-growing red tide, comprised mainly of Gonyaulax polyedra, were evaluated in limited trials of rat feeding. The protein of red tide (25 to 30 percent, dry basis) supported growth satisfactorily. The essential amino acid composition of the protein closely resembles that of casein, the major protein of milk. As a marine resource, plankton represents a challenge for research.
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTFerripolyphosphate-whey protein powders. Their potential as nutritional iron supplementsSusan B. Jones, Edwin B. Kalan, Thomas C. Jones, J. Frederic. Hazel, Locke F. Edmondson, Albert N. Booth, and James C. FritzCite this: J. Agric. Food Chem. 1975, 23, 5, 981–984Publication Date (Print):May 1, 1975Publication History Published online1 May 2002Published inissue 1 May 1975https://pubs.acs.org/doi/10.1021/jf60201a037https://doi.org/10.1021/jf60201a037research-articleACS PublicationsRequest reuse permissionsArticle Views98Altmetric-Citations11LEARN 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
Summary The genetic variants of cow β-lactoglobulin are indistinguishable by Ouchterlony double diffusion and the quantitative precipitin test. They are distinguishable from each other by complement and micro-complement fixation tests. Goat and sheep β-lactoglobulins are identical to the cow β-lactoglobulin variants by the Ouchterlony test, but are distinguishable by quantitative precipitation, complement and micro-complement fixation. Chemical modification of cow β-lactoglobulin, such as cleavage of the -His-Ile C-terminal sequence of the B variant, crystallization of the A variant with 2 moles of SDS and blocking of the -SH groups of the B variant with DTNB, do not produce molecules which are immunologically distinguishable from the parent molecule.
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