Characterization of monoclonal antibodies to oat phytochrome by competitive radioimmunoassays and comparative immunoblots of phytochrome peptides

Silberman, Lynn G.; Datta, Neeraj; Hoops, Pepper; Roux, Stanley J.

doi:10.1016/0003-9861(85)90614-9

Cited by 10 publications

(3 citation statements)

References 18 publications

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“…Procedures for preparation of P3·63 Ag 8 653 mouse myeloma cells (10 7 ) from American Type Cell Culture (Rockville, MD, USA), fusion with mice spleen cells (10 8 ), hybrid selection, and hybrid growth were essentially as described by Galfre et al (1977) and Silberman et al (1985) with some modifications. The ''parent'' hybrid cells were initially grown and cloned in 96-well plates using non-immunized mouse peritoneal macrophages (10 5 ) as the feeder layer.…”

Section: Electrophoresis and Immunoblottingmentioning

confidence: 99%

Biochemical and immunological characterization of pea nuclear intermediate filament proteins

Blumenthal

Clark

Roux

2004

Planta

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In immunoblot assays, at least three putative nuclear intermediate filament (NIF) proteins were detected in nuclear envelope-matrix (NEM) and lamin (L1) fractions of nuclei from plumules of dark-grown pea (Pisum sativum L.) seedlings. These NIF proteins had apparent molecular masses of ca. 65, 60, and 54 kDa (also referred to as p65, p60, and p54), and appeared as multiple isoelectric forms, with pIs ranging from ca. 4.8 to 6.0. Polyclonal and monoclonal antibodies were raised to the 65-kDa NIF protein bands excised from gels after electrophoresis. These anti-pea antibodies were specifically cross-reactive with the pea nuclear p65, p60, and p54 proteins and also with chicken lamins. Sequence alignment of peptide fragments obtained from the 65- and 60-kDa pea NIF proteins showed similarity with animal intermediate filament proteins such as lamins and keratins and with certain plant proteins predicted to have long coiled-coil domains. These pea NIF proteins were further purified and enriched from the NEM fraction using methods similar to those used for isolating animal lamins. When negatively stained and viewed by transmission electron microscopy, the filaments in the pea lamin (L1) fraction appeared to be 6-12 nm in diameter. As assayed by immunofluorescence cytochemistry using a confocal laser-scanning microscope, fixed pea plumule cells displayed uniform as opposed to peripheral nuclear staining by several of the antibody preparations, both polyclonal and monoclonal. This report describes the biochemical and immunological properties of these pea NIF proteins.

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Section: Electrophoresis and Immunoblottingmentioning

confidence: 99%

Biochemical and immunological characterization of pea nuclear intermediate filament proteins

Blumenthal

Clark

Roux

2004

Planta

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“…With the advent of new molecular probes of phytochrome structure including monoclonal antibodies Daniels and Quail, 1984;Thomas et d . , 1984b;Silberman et al, 1985) and phytochrome cDNA probes (Hershey et al, 1984), questions regarding structure and expression of multiple forms of phytochrome in plant tissue have now been directly addressed experimentally. Within the same tissue, evidence for multiple species of phytochrome in etiolated A vena seedlings was reported (Jordan et al, 1984).…”

Section: Multiple Species Of Phytochromementioning

confidence: 99%

Progress in the Molecular Analysis of Phytochrome

Lagarias

1985

Photochem & Photobiology

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“…30). Indeed, monoclonal antibodies have been useful in characterizing several plant proteins including 5-aminolevulinate dehydratase (18), an auxin transport carrier (14), nitrate reductase (6), and phytochrome (9,10,24).…”

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Production, Characterization, and Applications of Monoclonal Antibodies Reactive with Soybean Nodule Xanthine Dehydrogenase

Triplett¹,

Lending²,

Gumpf³

et al. 1986

Plant Physiol.

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Characterization of monoclonal antibodies to oat phytochrome by competitive radioimmunoassays and comparative immunoblots of phytochrome peptides

Cited by 10 publications

References 18 publications

Biochemical and immunological characterization of pea nuclear intermediate filament proteins

Biochemical and immunological characterization of pea nuclear intermediate filament proteins

Progress in the Molecular Analysis of Phytochrome

Production, Characterization, and Applications of Monoclonal Antibodies Reactive with Soybean Nodule Xanthine Dehydrogenase

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