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PubMed2026

Nourishing collaboration: interdisciplinary nutrition education for health care professionals.

Nutrition education remains insufficient in many health care professional training programs despite the central role of diet in the prevention and management of chronic disease. Contemporary nutrition science increasingly recognizes that dietary behaviors and health outcomes are shaped by complex interactions among biological, behavioral, environmental, and food system factors. This perspective proposes an interdisciplinary framework for nutrition education that integrates the complementary expertise of physicians, dietitians, chefs, and farmers. By bridging clinical care, nutrition science, culinary practice, and agricultural systems, such an approach may strengthen the translation of evidence into practice, improve nutrition-related competencies among health care professionals, and ultimately enhance population health outcomes.

Humans↗

PubMed1979

The presence of minor histone components in the chromatin of Pisum sativum L. seedlings.

Two minor basic protein components (M1 and M2) were found in the histone extract from chromatin of pea seedlings. In the histone extract of pea cotyledons only one minor component (M1) was detected. These minor components show a high affinity for chromatin, have a molecular weight of 20.200 and 17.800 respectively and a basic amino acid composition. They are not contaminants of cytoplasmatic origin. Two similar minor components were found in the chromatin of Pisum arvense and Lens culinaris-seedlings, one component was present in the chromatin from cotyledons of these species.

Amino Acids↗

PubMed1978

Common ancestor for concanavalin A and lentil lectin?

The primary structure of the alpha subunit from Lens culinaris lectin was determined by analysis of tryptic peptides and was shown to consist of 52 amino acid residues. The molecular weight calculated on the basis of the sequence is 5928. The whole chain is homologous with the region between positions 75 and 121 from concanavalin A. The NH2-terminal sequence of the beta chain, determined by automated Edman degradation, is homologous to another portion of the concanavalin A molecule, between positions 123 and 165. Comparison of the 94 residues from the lentil lectin alpha and beta chains with concanavalin A reveals the existence of 43 identities. Thirty-four other homologies could have arisen, each by a single nucleotide substitution. This extensive homology suggests that the lentil lectin alpha and beta chains may be proteolytic fragments from a single polypeptide chain of the same length as concanavalin A.

Amino Acid Sequence↗