Secondary structure of globulins from plant seeds: a re-evaluation from circular dichroism measurements

Zirwer, Dietrich; Gast, Klaus; Welfle, Heinz; Schlesier, Bernhard; Schwenke, K. D.

doi:10.1016/0141-8130(85)90039-x

Cited by 59 publications

(41 citation statements)

References 31 publications

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“…This observation agrees well with the secondary structure of globulins from plants seeds (11S from Brasica Napus L.; 11S from Helianthus annuus L.; 11S from Vicia faba; 7S from Phaseolus vulgaris L.) [16].…”

Section: Spectroscopic Measurementssupporting

confidence: 78%

Isolation, Biochemical Characterization, Oxido-Reductive and Proteolytic Activities of Globulin Protein Isolates from Seeds of Chia

Molina-Tizo¹,

Victoria²,

Soriano-Garcı́a³

2017

JAPLR

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Selective isolation, purification, secondary structure and functional properties of some globulins of Chia (Salvia hispanica L.) were studied. These globulins were isolated using water and two different NaCl concentrations (5 and 10%) and testing four enzymatic assays: polyphenol oxidase, catalase, peroxidase and chymoprotease for each extraction. Maximum protein extraction (18.4%) and highest enzymatic activity occurred in the presence of 5% NaCl. The main globulin protein was obtain using gel filtration chromatography and shows an increase of polyphenol oxidase, chymoprotease and proteolytic activities; and a decrease of catalase activity as compared with the crude extract. Further purification using anion-exchange chromatography produces two globulins SB1Q2 and SB1Q3 with molecular weights of 10 and 13 kDa and isoelectric points of 4.5 and 6.8, respectively. Their secondary structure using circular dichroism showed 42, 7%; 42.1, 7.4% of β-sheet and helical structures, respectively. This observation agrees well with the secondary structure of globulins in plant dicotyledonous seeds.

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Section: Spectroscopic Measurementssupporting

confidence: 78%

Isolation, Biochemical Characterization, Oxido-Reductive and Proteolytic Activities of Globulin Protein Isolates from Seeds of Chia

Molina-Tizo¹,

Victoria²,

Soriano-Garcı́a³

2017

JAPLR

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“…4A). These features of the spectrum are sufficient indicators of a highly ordered structure, including the a-helices and b types (Yang, Wu, & Martinez, 1986;Zirwer, Gast, Welfle, Schlesier, & Schwenke, 1985). In general, the CD spectrum of a-helix has an intense positive band at 191-193 nm and a typical double minimum at 208-210 and 222 nm, whilst that of bsheet has a fairly intense positive band at 195-200 nm and a negative band at about 216-218 nm (Yang et al, 1986).…”

Section: Secondary Conformationmentioning

confidence: 97%

Physicochemical and structural characterisation of globulin and albumin from common buckwheat (Fagopyrum esculentum Moench) seeds

Tang

Wang

2010

Food Chemistry

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“…The secondary structure of the rapeseed globulin determined by circular dichroism (CD) measurement is characterized by a low content (1 1 %) of helix and a relatively high content of jl-sheet conformation (about 30 %) [8]. More recently, the reevalution of the CD spectra using improved basis spectra gave 46-50 % p-conformation [9]. Taking into account the high content of p-conformation in the other 11 S plant seed globulins amounting to 42 % in helianthinin from sunflower and 39 % in legumin from faba beans, for example, one can conclude that this group of proteins belongs to the class of P-sheet proteins.…”

Section: Fig 1 Lsoelectric Focusing Of the 12 S Globulin From Rapesmentioning

confidence: 99%

Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins

Schwenke

1990

Nahrung

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Recent data on the structure and chemical modification of the two main storage proteins of rapeseed, the high-molecular mass 12 S globulin and the low-molecular mass 2 S protein (napin) are summarized and compared with those of related seed proteins. The 12 S globulin is built up of six subunits forming a quaternary structure which can be approximated by the model of a trigonal antiprism. The subunits, composed of a larger and a smaller polypeptide chain each, have a two-domain structure which is typical for all related plant proteins. These are characterized by a sedimentation coefficient of 11-13 S, a molecular mass of 300,000-360,000 g/mol and a high percentage of beta-sheet conformation. Increasing succinylation results in a step-by-step dissociation up to the subunits and to an unfolding of the latter at a critical level of modification amounting to 60-70%. These structural changes affect the functional properties remarkably. The napin fraction comprises a group of closely related and highly basic proteins with molecular masses of 12,000-14,000 g/mol, a high content of sulphur-containing amino acids and rich in helical conformation. They are built up of a larger and a smaller disulphide bridged polypeptide chain. Acylation does not abolish the secondary or tertiary structure which are stabilized by inter- and intrachain disulphide bonds. Acylation results, however, in a stabilization of the protein against heat-induced aggregation.

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Secondary structure of globulins from plant seeds: a re-evaluation from circular dichroism measurements

Cited by 59 publications

References 31 publications

Isolation, Biochemical Characterization, Oxido-Reductive and Proteolytic Activities of Globulin Protein Isolates from Seeds of Chia

Isolation, Biochemical Characterization, Oxido-Reductive and Proteolytic Activities of Globulin Protein Isolates from Seeds of Chia

Physicochemical and structural characterisation of globulin and albumin from common buckwheat (Fagopyrum esculentum Moench) seeds

Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins

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