Literature DB >> 16663655

A rapid, sensitive method for quantitating subunits in purified ribulose bisphosphate carboxylase preparations.

T J Andrews1, B Ballment.   

Abstract

Studies of the interactions of the large and small subunits of ribulose bisphosphate carboxylase require a knowledge of the concentrations of the subunits present in various preparations and their ratio. Since existing sodium dodecyl sulfate-gel electrophoresis procedures proved quantitatively unreliable, a technique based on high performance-gel filtration was developed. The latter is most reliable, takes only about 30 minutes to perform, and detects a minimum of 0.25 micrograms of each subunit.

Entities:  

Year:  1984        PMID: 16663655      PMCID: PMC1066941          DOI: 10.1104/pp.75.2.508

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  10 in total

1.  Molecular cloning and sequence analysis of the cyanobacterial gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase.

Authors:  K Shinozaki; C Yamada; N Takahata; M Sugiura
Journal:  Proc Natl Acad Sci U S A       Date:  1983-07       Impact factor: 11.205

2.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

3.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors:  M M Bradford
Journal:  Anal Biochem       Date:  1976-05-07       Impact factor: 3.365

4.  Estimation of the molecular weight of ribulose diphosphate carboxylase sub-units.

Authors:  A C Rutner
Journal:  Biochem Biophys Res Commun       Date:  1970-06-05       Impact factor: 3.575

5.  Measurement of molecular weights by electrophoresis on SDS-acrylamide gel.

Authors:  K Weber; J R Pringle; M Osborn
Journal:  Methods Enzymol       Date:  1972       Impact factor: 1.600

6.  The function of the small subunits of ribulose bisphosphate carboxylase-oxygenase.

Authors:  T J Andrews; B Ballment
Journal:  J Biol Chem       Date:  1983-06-25       Impact factor: 5.157

7.  Kinetics and subunit interactions of ribulose bisphosphate carboxylase-oxygenase from the cyanobacterium, Synechococcus sp.

Authors:  T J Andrews; K M Abel
Journal:  J Biol Chem       Date:  1981-08-25       Impact factor: 5.157

8.  Carbon dioxide assimilation in blue-green algae: initial studies on the structure of ribulose 1,5-bisphosphate carboxylase.

Authors:  F R Tabita; S E Stevens; J L Gibson
Journal:  J Bacteriol       Date:  1976-02       Impact factor: 3.490

9.  Purification, quaternary structure, composition, and properties of D-ribulose-1,5-bisphosphate carboxylase from Thiobacillus intermedius.

Authors:  K Purohit; B A McFadden; A L Cohen
Journal:  J Bacteriol       Date:  1976-07       Impact factor: 3.490

10.  Protein liganding to the activator cation of ribulosebisphosphate carboxylase.

Authors:  H M Miziorko; C E Behnke; E C Houkom
Journal:  Biochemistry       Date:  1982-12-21       Impact factor: 3.162

  10 in total
  1 in total

1.  Artificially evolved Synechococcus PCC6301 Rubisco variants exhibit improvements in folding and catalytic efficiency.

Authors:  Dina N Greene; Spencer M Whitney; Ichiro Matsumura
Journal:  Biochem J       Date:  2007-06-15       Impact factor: 3.857

  1 in total

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