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Changes of subunit structure on heat-induced precipitation of 12 S globulin from repeseed (Brassica napus L.) (Short communication)

✍ Scribed by Gwiazda, St. ;Schwenke, K. D.

Publisher: John Wiley and Sons
Year: 1984
Tongue: English
Weight: 254 KB
Volume: 28
Category: Article
ISSN: 0027-769X
DOI: 10.1002/food.19840280515

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✦ Synopsis

The polypeptide chain pattern of the rapeseed 12 S globulin i n the SDS gel electrophoresis is characterized by 4 main zones P X l , P E 2 , PpC3 and PPC4 with molecular masses of 18500, 21000, 27000 and 31000 D re8 ectively (1). Some of them split into double bands (Fig. ) 72).

It wa8 suggested that each small zone (PPC1 or PpC2) combines with one larger zone (PpC3 or Ppc4) to form a "50000 D protomer" in the hexameric structure of the na-

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Diameter estimation of 12 S globulin mol

Diameter estimation of 12 S globulin molecules from rapeseed (Brassica napus L.) by means of electron microscopy using the freeze-drying technique in combination with Pt/Pd-shadowing (Short communication)

✍ Titova, E. F. ;Belavtseva, E. M. ;Schwenke, K. D. 📂 Article 📅 1985 🏛 John Wiley and Sons 🌐 English ⚖ 469 KB 👁 1 views

The 12 S globulin is an oligomeric storage protein in rapeseed with a molecular weight of 300 000 g . m1-l (1, 2 ) . Its molecular shape and quaternary structure has been investigated by means of small-angle X-ray scattering and by electron microscopy after negative staining (2 -4). The object