Characterization of an immunoglobulin binding protein homolog in the maize floury-2 endosperm mutant.

Fontes, Elizabeth B. P.; Shank, Brain B.; Wrobel, Russell L.; Moose, Stephen P.; OBrian, Gregory R.; Wurtzel, Eleanore T.; Boston, Rebecca S.

doi:10.1105/tpc.3.5.483

Cited by 162 publications

(25 citation statements)

References 42 publications

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“…It was demonstrated by molecular cloning technique that hsp70-1ike proteins are common in plants [13,21,29,37,38,46]. In this report, we show that a protein with M r = 73 000 has been purified from cytosol of mung bean seeds by DEAE-cellulose and ATP-agarose chromatography.…”

Section: Discussionmentioning

confidence: 79%

“…Comparison among predicted amino acid sequences of the cloned genes shows that the hsp70-1ike proteins in plants [13,21,29,37,38,46] and the hsc70 in bovines [ 11] and in rats [35] are highly homologous. Therefore, one would expect that antibodies made against bovine hsc70 would cross-react with hsp70-1ike gene products in plants.…”

Section: Antibodies Against Bovine Hsc70 Recognize 70 Kda Heat Shock mentioning

confidence: 99%

“…Clathrin-uncoating ATPase (hsc70) promotes dissociation of clathrins from coated vesicles [12,39]. BiP has been implicated to catalyze protein folding and subunit assembly in endoplasmic reticulum for both animal and plant systems [2,13,21,24,43, for a review, see 36]. Gao et al [22] reported recently that SSA1 and SSA2 proteins in yeast also possess clathrin-uncoating activity.…”

Section: Introductionmentioning

confidence: 99%

“…Although several hsp70-1ike genes in plants have been cloned and sequenced [13,21,29,37,38,46], biochemical characterization of these proteins is generally lacking. Since a thorough understanding of the biochemical properties of hsc70 is essential for elucidating its physiological role, we undertook to purify and to characterize hsp70-1ike proteins from mung bean seeds and young seedlings.…”

Section: Introductionmentioning

confidence: 99%

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The disappearance of an hsc70 species in mung bean seed during germination: purification and characterization of the protein

Wang

Lin

1993

Plant Mol Biol

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We have purified a 73 kDa protein from the cytosolic fraction of mung bean seeds. It comprises 0.5-1% of the total protein in seeds. This purified protein is a bona fide hsc70 on the basis of several lines of evidence. First, antibodies against bovine brain hsc70 cross-react with the purified 73 kDa protein. Second, the purified protein comigrates on two-dimensional gels with one of the heat-inducible hsc70s in mung bean seedlings. Third, similar to other hsc70 species, the purified 73 kDa protein has a high affinity for ATP. Finally, the hydrolysis of ATP by the purified protein can be stimulated by peptides; ATPase activity increases from 40 nmol/h to 165 nmol/h per mg of protein. The purified mung bean hsc70 autophosphorylates at a substoichiometric level. Moreover, the amount of this hsc70 species diminishes while new species of hsc70s appear after germination, suggesting that the expression of hsc70 in mung bean is subject to developmental regulation.

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Section: Discussionmentioning

confidence: 79%

Section: Antibodies Against Bovine Hsc70 Recognize 70 Kda Heat Shock mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The disappearance of an hsc70 species in mung bean seed during germination: purification and characterization of the protein

Wang

Lin

1993

Plant Mol Biol

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“…Modifications of the methods of Fontes et al [20] and Larkins and Hurkman [42] were used to purify endoplasmic reticulum. Leaf tissue was ground with a mortar and pestle in grinding buffer (10 mM Tris-HC1 pH 8.5 at 25 °C, 7.2~ sucrose (w/v), 10 mM KCI, 5 mM MgC12).…”

Section: Endoplasmic Reticulummentioning

confidence: 99%

Characterization of a spinach gene responsive to low temperature and water stress

et al. 1993

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The characterization of a cDNA for an 85 kDa spinach protein, CAP85 (cold acclimation protein) that is responsive to cold acclimation and water stress is described. Both transcript and protein levels are increased during cold acclimation and water stress. A novel characteristic of CAP85 is the presence of an 11 amino acid, lysine-rich repeat, common to Group 2 LEAs (late embryogenesis abundant proteins), which is included within a larger repeating motif present in 11 copies. Two other motifs of 8 and 16 residues are also found in three and four copies, respectively. CAP85 like other dehydrins and cold-regulated polypeptides remains soluble upon boiling. Protein blot analyses indicate that CAP85 protein is expressed in all aerial tissues as well as in roots. RNA blots show the presence of mRNA for the 85 kDa protein in leaf, petiole, and root tissue. Cell fractionation studies suggest that CAP85 is predominantly found in the cytosol.

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Production of monoclonal antibodies by tobacco hairy roots

Wongsamuth

Doran

1997

Biotechnol. Bioeng.

147

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Hairy roots of tobacco (Nicotiana tabacum) were used to produce full‐length murine lgG1 monoclonal antibody. The presence of heavy (γ) and light (κ) chains and fully assembled antibody was verified by Western blot analysis of root extracts. Antibody levels in the biomass and medium were quantified by ELISA based on detection of γ‐κ complexes. Antibody produced by hairy roots was fully functional as demonstrated in bacterial aggregation assays which confirmed bivalent antigen‐binding capacity. Eight antibody‐producing hairy root clones retained their ability to produce mouse immunoglobulin over a period of 19 months after transformation with Agrobacterium rhizogenes. For hairy roots grown in Gamborg's B5 medium, the maximum level of assembled antibody after 21‐day culture in shake flasks was 18 mg L−1 or 1.8% total soluble protein; up to 14% of the antibody was secreted into the medium. Antibody production by transgenic hairy roots had a negligible effect on growth compared with hairy roots of wild‐type tobacco. Antibody accumulation was growth associated with constant specific accumulation rate at the beginning of the culture; however, degradation of antibody was significant after 14 days and the amount of assembled antibody declined. Unlike hybridoma cultures, the time course of antibody accumulation by hairy roots showed a distinctive maximum very soon after the end of exponential growth. Total antibody levels were increased by addition of nitrate, polyvinylpyrrolidone, or gelatin to the medium. Polyvinylpyrrolidone and gelatin also markedly improved extracellular antibody concentrations; with these treatments, up to 43% of the antibody present was secreted into the medium. Antibody production was tested using hairy roots grown in an air‐driven bioreactor. The intracellular antibody content after 30‐day bioreactor culture was similar to that measured in shake flasks; however, the final extracellular antibody level was 1.7 times higher than the maximum measured in shake flasks. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 54: 401–415, 1997.

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Characterization of an immunoglobulin binding protein homolog in the maize floury-2 endosperm mutant.

Cited by 162 publications

References 42 publications

The disappearance of an hsc70 species in mung bean seed during germination: purification and characterization of the protein

The disappearance of an hsc70 species in mung bean seed during germination: purification and characterization of the protein

Characterization of a spinach gene responsive to low temperature and water stress

Production of monoclonal antibodies by tobacco hairy roots

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