Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure-physicochemical function relationships of soybean beta-conglycinin constituent subunits.

Journal of agricultural and food chemistry - 1 Dec 1999

Maruyama N, Sato R, Wada Y, Matsumura Y, Goto H, Okuda E, Nakagawa S, Utsumi S

Abstract excerpt

Beta-conglycinin, one of the dominant storage proteins of soybean, has a trimeric structure, being composed of three subunits alpha, alpha', and beta. The alpha and alpha' subunits contain the extension regions in addition to the core regions common to all subunits, which are N-glycosylated. Physicochemical functions of recombinant nonglycosylated individual subunits and deletion mutants (alpha(c) and alpha'(c))...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antigens, Plant
Share to Fluorescence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glycine max

Share to Hot Temperature

Share to Seed Storage Proteins

Share to Solubility

Share to Soybean Proteins

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 10606609
DOI: 10.1021/jf990360+

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure-physicochemical function relationships of soybean beta-conglycinin constituent subunits.PMID 10606609Read ↗

The roles of the N-linked glycans and extension regions of soybean beta-conglycinin in folding, assembly and structural features.Semantic proximity Read ↗

Structure of the core region of the soybean beta-conglycinin alpha' subunit.Semantic proximity Read ↗

Molecular analysis and physicochemical properties of electrophoretic variants of wild soybean Glycine soja storage proteins.Semantic proximity Read ↗

Polypeptide modification: an improved proglycinin design to stabilise oil-in-water emulsions.Semantic proximity Read ↗

Improvement of nutritional value and functional properties of soybean glycinin by protein engineering.Semantic proximity Read ↗

C-terminus engineering of soybean proglycinin: improvement of emulsifying properties.Semantic proximity Read ↗

Characterization of beta-conglycinin and glycinin soy protein fractions from four selected soybean genotypes.Semantic proximity Read ↗

Genotypic influence on soybean protein quality: Linking molecular structure, functional properties, and nutritional quality through principal component and correlation analyses.Semantic proximity Read ↗

Processing and assembly in vitro of engineered soybean beta-conglycinin subunits with the asparagine-glycine proteolytic cleavage site of 11S globulins.Semantic proximity Read ↗

Development of transgenic rice containing a mutated beta subunit of soybean beta-conglycinin for enhanced phagocytosis-stimulating activity.Semantic proximity Read ↗

Wheat seed storage proteins: Advances in molecular genetics, diversity and breeding applicationsSemantic proximity Read ↗

Genetic mapping and validation of the loci controlling 7S α' and 11S A-type storage protein subunits in soybean [Glycine max (L.) Merr.].Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.