Isolation of glycinin subunits by isoelectric focusing in urea‐mercaptoethanol

Catsimpoolas, Nicholas

doi:10.1016/0014-5793(69)80249-8

Cited by 78 publications

(36 citation statements)

References 9 publications

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“…The 11S globulin purified by our method at least showed a dissociation reaction as an intrinsic property at a slightly alkaline pH at a low ionic strength as observed by Wolf et al10) in sedimentation. Thus, we agree that the most stable form of 11S globulin is the dimer form as suggested by Catsimpoolas et al 1) From the above results and the discussion, it is proposed that 11S globulin consists of two similar, but not identical monomers; either monomer containing three intermediary subunits consists of one mole of either A1 or A2, one mole of A3, one mole of A4, one mole of either B1 or B2, one mole of B3 and one mole of B4. Thus, the dimer (11S globulin molecule) should exhibit a molecular weight of 362,000 due to the molecular weights of the intermediary subunits estimated by SDS gel electrophoresis, or a molecular weight of 373,000 due to the subunit molecular weights estimated by SDS gel electrophoresis.2) These values are in a relatively good agreement with the value of 363,00011, reported.…”

Section: Fractionation Of Intermediary Subunitsupporting

confidence: 91%

Subunit structure of soybean 11S globulin.

Kitamura

Takagi

Shibasaki

1976

Agricultural and Biological Chemistry

103

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The acidic and the basic subunits were shown to be present in equimolar amounts in the 11S globulin molecule by the densitometric scanning of the SDS gel and the molecular weight consideration.The four acidic subunits (A1, A2, A3 and A4) were found to be present in the approximate molar ratio of 1:1:2:2. Four basic subunits separated and designated as Bl, B2, B3 and B4 based on the relative mobilities in the acidic gel in 7M urea were found to be present in the approximate molar ratio of 1:1:2:2.The four basic subunits were fractionated in approximately same amounts into three different peaks, peak I (B1 and B2), peak II (B3) and peak III (B4) by CM-Sephadex C-50 column chromatography in the presence of 6M urea. Three kinds of intermediary subunits of 11S globulin were fractionated with DEAE-Sephadex A-50 in the absence of reducing agents in 6M urea, and disulfide bonds appeared to participate in the binding between the acidic and the basic subunits in the molar ratio of 1:1 with the following combinations; A1 and A2 combined with B3, A3 with Bi and B2, and A4 with B4. In view of the above results and molecular weight consideration, a new model of subunit structure was proposed for 11S globulin. Catsimpoolaset al

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Section: Fractionation Of Intermediary Subunitsupporting

confidence: 91%

Subunit structure of soybean 11S globulin.

Kitamura

Takagi

Shibasaki

1976

Agricultural and Biological Chemistry

103

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“…seeds, is a hexameric protein which has an A4, of -360 000 and a sedimentation coefficient (szo,,,,) of -12 [1,2]. Each of the 6 subunits in a glycinin molecule is composed of an acidic (Mr 35 000-42 000) polypeptide and a basic (Mr 22000) polypeptide [2-41.…”

Section: Introductionmentioning

confidence: 99%

A complete cDNA coding for the sequence of glycinin A₂B_1a subunit precursor

Momma¹,

Negoro²,

Udaka³

et al. 1985

FEBS Letters

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Analysis of the A2B,. subunit precursor, one of the AZ-subunit family of glycinin, the main storage protein of soybean, revealed that it is composed of a signal peptide segment (18 amino acids), the A2 acidic polypeptide (282 amino acids), followed by the B,. basic polypeptide (185 amino acids). There was overall 63% homology between this subunit complex and pea legumin, which is an analogous protein to glycinin. As this degree of homology is rather higher than that in the A,B, subunit, one of the A, subunit family, it seems that the genes encoding the A2 subunit family are phylogenetically more strongly related to the legumin genes. Soybean I1 S storage protein Glycinin

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“…[2][3][4][5][6][7] On the other hand, differences of subunit composition among cultivars have been found in major components of the seed storage proteins of soybean,S) ground nut,9) lupin iol and pea.…”

Section: )mentioning

confidence: 99%