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Plant Mol. Biol. 28, 369-380. Isolation and characterisation of cDNA clones representing the genes encoding the major tuber storage protein (dioscorin) of yam (Dioscorea cayenensis Lam.). 1995

Conlan, R. S. , Griffiths, L. A. , Napier, J. A. , Shewry, P. R. , Mantell, S. , Ainsworth, C.

Notes: The cDNA for dioscorin was expressed using the TNT® Coupled Reticulocyte Lysate System. When translation was carried out in the presence of canine microsomes, the translation efficiency was increased and a band of faster mobility was produced. Dioscorin may be cotranslationally processed by cleavage of a signal peptide; in addition, other post-translational modifications (i.e., glycosylation) may occur with this protein. (1273)

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J. Biol. Chem. 270, 29439-29446. Molecular cloning, expression and characterization of podocalyxin-like protein 1 from rabbit as a transmembrane protein of glomerular podocytes and vascular endothelium. 1995

Kershaw, D.B., Thomas, P.E., Wharram, B.L., Goyal, M., Wiggins, J.E., Whiteside, C.I. and Wiggins, R.C.

Notes: Reactions were performed in 25µl reactions with or without 1.5µl of microsomes. The 551 residue protein had a putative signal sequence and N-linked glycosylation sequences. Expression in the presence of the microsomes did produce an increase in molecular weight. (1623)

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J. Immunol. 150, 4920-4927. Expression cloning of the early activation antigen CD69, a type II integral membrane protein with a C-type lectin domain. 1993

Hamann, J., Fiebig, H., Strauss, M.

Notes: Early activation antigen CD69 was expressed using the TNT® Coupled Reticulocyte Lysate System. Cotranslational processing was investigated using Canine Pancreatic Microsomal Membranes. The two cotranslationally processed products of 28kDa and 34kDa are the different glycosylated forms of the protein. (1057)

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