scholarly journals The cDNA cloning of a pea (Pisum sativum) seed lipoxygenase. Sequence comparisons of the two major pea seed lipoxygenase isoforms

1989 ◽  
Vol 264 (3) ◽  
pp. 929-932 ◽  
Author(s):  
P M Ealing ◽  
R Casey
Keyword(s):  
Glycine Max ◽  
Amino Acid ◽  
Pisum Sativum ◽  
Amino Acid Sequence ◽  
Cdna Cloning ◽  
Soya Bean ◽  
Its Sequence ◽  
Cloning And Sequencing ◽  
Sequence Comparisons ◽  
Pea Seed

Cloning and sequencing of two cDNAs from mRNA of maturing pea (Pisum sativum) seeds allowed the deduction of the complete amino acid sequence of a lipoxygenase polypeptide which is most similar to that of soya-bean lipoxygenase 2. The predicted Mr of this polypeptide is 97134, and its sequence permits comparisons between the lox2-type and the lox3-type lipoxygenase isoforms from pea and soya bean (Glycine max).

scholarly journals Purification from Placenta, Amino Acid Sequence, Structure Comparisons and cDNA Cloning of Human Glutaredoxin

1995 ◽  
Vol 227 (1-2) ◽  
pp. 27-34 ◽  
Author(s):  
C. Alicia Padilla ◽  
Emilia Martinez-Galisteo ◽  
J. Antonio Barcena ◽  
Giannis Spyrou ◽  
Arne Holmgren
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Cloning ◽  
Sequence Structure

Identification and cDNA cloning of a Xenopus nucleolar phosphoprotein, xNopp180, that is the homolog of the rat nucleolar protein Nopp140

1995 ◽  
Vol 108 (10) ◽  
pp. 3339-3347 ◽  
Author(s):  
C. Cairns ◽  
B. McStay
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Cloning ◽  
Cdna Clone ◽  
Xenopus Oocyte ◽  
Ribosome Biogenesis ◽  
Nucleolar Protein ◽  
Nuclear Localisation Signal ◽  
Cdc2 Kinase

The monoclonal antibody G1C7, recognises both Xenopus nucleolin and a protein of 180 kDa present in Xenopus oocyte nucleoli. This antibody was used to obtain a cDNA clone encoding the 180 kDa protein now called xNopp180 (Xenopus nucleolar phosphoprotein of 180 kDa). Analysis of the deduced amino acid sequence from this cDNA shows that xNopp180 is almost entirely composed of alternating acidic and basic domains. We show that xNopp180 is heavily phosphorylated and that it contains multiple consensus sites for phosphorylation by casein kinase II and cdc2 kinase. In addition we show that xNopp180 is the 180 kDa antigen recognised by the monoclonal antibody No-114, thus allowing reinterpretation of previous work with this antibody. xNopp180 appears to be the Xenopus homolog of the rat nucleolar protein Nopp140. Nopp140 is a nuclear localisation signal binding protein that shuttles on curvilinear tracks between the nucleolus and the cytoplasm. Possible roles for xNopp180/Nopp140 in ribosome biogenesis are discussed.

Amino Acid Sequence Comparisons

1998 ◽  
pp. 30-33
Author(s):  
Jeffrey Griffith ◽  
Clare Sansom
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Comparisons

Natural 15N Abundance of NH4+, Amide N, and Total N in Various Fractions of Nodules of Peas, Soybeans and Lupins

1989 ◽  
Vol 16 (4) ◽  
pp. 305 ◽  
Author(s):  
G Shearer ◽  
DH Kohl
Keyword(s):  
Protein Synthesis ◽  
Glycine Max ◽  
Amino Acid ◽  
Pisum Sativum ◽  
Root Nodules ◽  
Lupinus Luteus ◽  
Total N ◽  
Isotope Discrimination ◽  
15N Enrichment ◽  
15N Abundance

Nodules of certain N2-fixing root nodules are substantially enriched in 15N compared with non-nodular tissues. This enrichment usually resides largely within bacteroids. Isotope discrimination associated with export of ammonia(um) from the bacteroid would result in 15N enrichment of NH4+ within bac- teroids. Bacteroid protein synthesis from this pool of 15N enriched NH4+ would then account for enrichment of the bacteroids. Measurements of 15N abundances of total N and free NH4+ in nodule fractions from lupins (Lupinus luteus), soybeans (Glycine max) and peas (Pisum sativum) showed this was not the case. With the inocula used in experiments reported here, lupin and soybean nodules were enriched in 15N, while pea nodules were not. There was no correlation between 15N abundances of NH4+ and total N in the nodule fractions (r= 0.445, P> 0.2). We conclude that isotope discrimination associated with ammonia(um) transport does not explain the 15N elevation of lupin and soybean nodules. We also conclude, on the basis of the large isotope effect for the equilibrium between NH4+ and NH3, that most of the ammonia(um) is exported from bacteroids as NH4+ rather than NH3. We also measured the 15N abundance of free amide N. There was a strong correlation between 15N abundances of free amide N and total N in nodule fractions (r=0.924, P<0,001), suggesting that amide N is a significant source of N to the amino acid pools from which proteins are synthesised.

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