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Characterisation of the major storage proteins of Pisum sativum L


, : Characterisation of the major storage proteins of Pisum sativum L. Characterisation of the major storage proteins of Pisum sativum L: 205

Purification techniques for isolating the storage proteins vicilin and legumin from pea seeds were studied.

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Gatehouse, J.A.; Croy, R.R.; Morton, H.; Tyler, M.; Boulter, D., 1981: Characterisation and subunit structures of the vicilin storage proteins of pea (Pisum sativum L.). Investigations of the vicilin fraction of the storage proteins of pea (Pisum sativum L.) have shown that its major components are a number of protein species of Mr 170 000. Convicilin (Mr 280 000, composed of 71 000-Mr subunits) is a separable com...

Croy, R.R.D.; Gatehouse, J.A.; Evans, I.M.; Boulter, D., 1980: Characterisation of the storage protein subunits synthesized in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.). Evidence is presented to show that legumin, the major storage protein in peas, was synthesized in vitro by the wheat germ and reticulocyte lysate systems from polyribosomes and mRNA isolated from developing pea seeds. While legumin isolated from m...

Hinz, G.; Hoh, B.; Hohl, I.; Robinson, D.G., 1995: Stratification of storage proteins in the protein storage vacuole of developing cotyledons of Pisum sativum L. Legumin, vicilin and pea albumin are the most prominent storage proteins in pea seeds. In order to localize these proteins in the developing cotyledons we have employed an improved fixation procedure for immunogold labelling for electron microscop...

Croy, R.R.; Gatehouse, J.A.; Evans, I.M.; Boulter, D., 1980: Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.) : I. Legumin. Evidence is presented to show that legumin, the major storage protein in Pisum, is synthesised in vitro by the wheat germ and reticulocyte lysate systems, from polyribosomes and mRNA isolated from developing pea seeds. While legumin isolated from...

Croy, R.R.D.; Gatehouse, J.A.; Evans, I.M.; Boulter, D., 1980: Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.) 2. Vicilin. Polypeptide material was immunoprecipitated by antivicilin antibodies from translation products of polyribosomes and poly(A)-rich RNA isolated from developing pea seeds in the wheat germ and reticulocyte lysate cell-free synthesis systems. Analysi...

Croy, R.R.; Gatehouse, J.A.; Marta Evans, I.; Boulter, D., 1980: Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.) : II. Vicilin. Polypeptide material has been immunoprecipitated by antivicilin antibodies from translation products of polyribosomes and poly(A)-rich RNA isolated from developing seeds of Pisum sativum in the wheat germ and reticulocyte lysate cell-free synthesi...

Wood, C.K.; Pratt, J.R.; Moore, A.L., 1998: Identification and characterisation of cultivar-specific 22-kDa heat shock proteins from mitochondria of Pisum sativum. Pea plants (Pisum sativum L. cv. Feltham First) exposed to a heat stress of 37degreeC for 6 h accumulated two low molecular weight (LMW) heat shock proteins (HSPs) of molecular mass 22 kDa. The two LMW HSPs were associated, with purified mitochond...

Thomson, J.A.; Schroeder, H.E.; Tassie, A.M., 1980: Cotyledonary storage proteins in pisum sativum 5. further studies on molecular heterogeneity in the vicilin series of holo proteins. The cotyledonary storage proteins of mature pea seeds were resolved by polyacrylamide gel electrophoresis in an acid buffer system as discrete bands comprising holoproteins referable to either the legumin or vicilin series. Three major and 4 less...

Wenzel, M.; Rudiger, H., 1995: Interaction of pea (Pisum sativum L.) lectin with pea storage proteins. The study of interactions between plant lectins and endogenous binding partners could assist in understanding the biological role of these proteins. From the storage proteins isolated from pea cv. Kleine Rheinlanderin seeds, a small but defined po...

Hassan, A.M.; Wesson, C.; Trumble, W.R., 1995: Calreticulin is the major Ca2+ storage protein in the endoplasmic reticulum of the pea plant (Pisum sativum). A 56kDa protein with high similarity in its N-terminal amino acid sequence to animal calreticulin and 100% homology with the N-terminal amino acids of spinach calreticulin has been identified in seeds of the pea plant (Pisum sativum). A new purifi...