scholarly journals The post-translational proteolysis of the subunits of vicilin from pea (Pisum sativum L.)

1982 ◽  
Vol 207 (3) ◽  
pp. 629-632 ◽  
Author(s):  
J A Gatehouse ◽  
G W Lycett ◽  
R R D Croy ◽  
D Boulter
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Pisum Sativum ◽  
Tryptic Peptide ◽  
Proteolytic Cleavage ◽  
Amino Acid Sequencing ◽  
Complementary Dna ◽  
Pisum Sativum L ◽  
Peptide Profiles

Tryptic-peptide profiles and amino acid sequencing of purified pea (Pisum sativum L.) vicilin subunits were used to show that their sequences were interrelated. Comparison with the nucleotide sequence of a cloned vicilin complementary DNA (mRNA) showed that all vicilin subunits could be derived from 50 000-Mr precursors containing up to two sites for post-translational proteolytic cleavage, and allowed these subunits to be located relative to the precursor.

scholarly journals Convicilin mRNA from pea (Pisum sativum L.) has sequence homology with other legume 7S storage protein mRNA species

1984 ◽  
Vol 224 (2) ◽  
pp. 661-666 ◽  
Author(s):  
R Casey ◽  
C Domoney ◽  
J Stanley
Keyword(s):  
Nucleotide Sequence ◽  
Pisum Sativum ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Nucleotide Sequence Analysis ◽  
Sequence Difference ◽  
Legume Seed ◽  
Complementary Dna ◽  
Pisum Sativum L

Nucleotide-sequence analysis of a complementary-DNA clone for convicilin, one of the storage proteins from pea (Pisum sativum L.) seeds, shows it to be homologous with the 7S legume seed storage proteins vicilin, conglycinin and phaseolin. Convicilin is more similar to vicilin than to phaseolin or to conglycinin. Significant areas of sequence difference are discussed.

Purification and partial amino acid sequencing of a mycorrhiza-related chitinase isoform from Glomus mosseae -inoculated roots of Pisum sativum L.

Planta ◽  
2001 ◽  
Vol 213 (5) ◽  
pp. 781-787 ◽  
Author(s):  
Sophie Slezack ◽  
Jonathan Negrel ◽  
Gw�na�lle Bestel-Corre ◽  
Eliane Dumas-Gaudot ◽  
Silvio Gianinazzi
Keyword(s):  
Amino Acid ◽  
Pisum Sativum ◽  
Glomus Mosseae ◽  
Amino Acid Sequencing ◽  
Pisum Sativum L

scholarly journals A novel giant secretion polypeptide in Chironomus salivary glands: implications for another Balbiani ring gene.

1985 ◽  
Vol 101 (3) ◽  
pp. 1044-1051 ◽  
Author(s):  
W Y Kao ◽  
S T Case
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Salivary Glands ◽  
Cyanogen Bromide ◽  
Tryptic Peptide ◽  
Amino Acid Sequences ◽  
The Other ◽  
Balbiani Ring ◽  
Sequence Organization ◽  
Peptide Maps

Chironomus salivary glands contain a family of high Mr (approximately 1,000 X 10(3)) secretion polypeptides thought to consist of three components: sp-Ia, sp-Ib, and sp-Ic. The use of a new extraction protocol revealed a novel high Mr component, sp-Id. Results of a survey of individual salivary glands indicated that sp-Id was widespread in more than a dozen strains of C. tentans and C. pallidivittatus. Sp-Id was phosphorylated at Ser residues, and a comparison of cyanogen bromide and tryptic peptide maps of 32P-labeled polypeptides suggested that sp-Ia, sp-Ib, and sp-Id are comprised of similar but nonidentical tandemly repeated amino acid sequences. We concluded that sp-Id is encoded by an mRNA whose size and nucleotide sequence organization are similar to Balbiani ring (BR) mRNAs that code for the other sp-I components. Furthermore, parallel repression of sp-Ib and sp-Id synthesis by galactose led us to hypothesize that both of their genes exist within Balbiani ring 2.

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