A simple and cheap remotely operated system for the iodination of proteins

Henville, A.; Jenkin, Graham

doi:10.1016/0003-2697(73)90034-1

Cited by 7 publications

(2 citation statements)

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“…The antigens were radioactively labelled with 125 Iodine (Amersham Buchler, Braunschweig, FRG) by the chloramine-T method (Henville and Jenkin, 1973). The labelled antigens were incubated with the different immune sera or the MAb for 15 hr at 8°C, then with the second antiserum directed against rabbit immunoglobulin (lg) (Dakopatts) or mouse lg (Dakopatts) for 4 hr at room temperature.…”

Section: Lmmunoprecipitationmentioning

confidence: 99%

Two Cea and Three Nca Species, Although Distinguishable by Monoclonal Antibodies, Have Nearly Identical Peptide Patterns

Fritz

Abuharfeil

Schwarz

et al. 1985

Intl Journal of Cancer

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In perchloric acid extracts of normal lung and colonic tumors, 3 NCA molecules were identified by monoclonal antibodies that cross-reacted with CEA, which itself gave 2 bands in SDS-PAGE. The proteins had molecular weights of 50, 75 and 97 kd, while the 2 CEA molecules banded at 180 and 160 kd in SDS-PAGE. No MAb recognized only one molecule, with the exception of MAb 3/13 which precipitated solely the upper CEA band. Analysis of the biochemical relationship of the cross-reactive antigens showed that none of them contained any internal methionine. Furthermore, after digestion by thermolysin, the peptide maps of the immunoprecipitated molecules showed very close similarities, if not identity. When the cross-reactive and the CEA were compared, the only differences found were in the upper CEA band, which apparently lacked one hydrophobic peptide, while the 97 kd cross-reacting protein showed one extra peptide. We conclude from our results that CEA and the cross-reacting molecules are composed of nearly identical, small (i.e. less than 50 kd) polypeptide chains.

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Section: Lmmunoprecipitationmentioning

confidence: 99%

Two Cea and Three Nca Species, Although Distinguishable by Monoclonal Antibodies, Have Nearly Identical Peptide Patterns

Fritz

Abuharfeil

Schwarz

et al. 1985

Intl Journal of Cancer

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“…Purified ovine LH (LER-1056-C2) was iodinated by the chloramine-T method of Greenwood, Hunter & Glover (1963) using a remotely operated system (Henville & Jenkin, 1973). Iodinated LH was separated from free iodine on a column of Sephadex G25 fine, 5x1 cm.…”

Section: Radioimmunoassay Oflhmentioning

confidence: 99%

Pituitary responsiveness to synthetic LH-RH and pituitary LH content at various reproductive stages in the sheep

Jenkin¹,

Heap²,

Symons³

1977

Reproduction

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In sheep the basal concentration of LH in jugular vein plasma was significantly higher during the first 50 days of gestation in late pregnancy or at parturition. The pituitary response to a single i.v. injection of 200 microng synthetic LH-RH was determined at different stages of gestation and compared with that of anoestrous and cyclic sheep. Pituitary response to LH-RH decreased progressively with advancing gestation: by 56 days after mating the response had declined to 35% and by parturition to 14% of the value in anoestrous sheep. The pituitary response to LH-RH increased after parturition and the pattern of recovery differed in non-lactating and lactating sheep. By 63 days postpartum the response to LH-RH in non-lactating and lactating animals had returned to values similar to those in sheep during anoestrus and sheep during the luteal phase of the oestrous cycle. A decrease in pituitary responsiveness during pregnancy was associated with a decrease in pituitary content of LH. The quantity of LH released in response to a standard injection of LH-RH was linearly related to pituitary LH content.

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Electroblotting of proteins on agarose gel containing specific antibodies

Atmeh

Abuharfeil

1993

Electrophoresis

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A method is described for electroblotting of proteins, separated by gradient polyacrylamide gel electrophoresis, onto an agarose gel matrix containing specific antibodies. Three proteins of different molecular weight, including human albumin, isolated and in plasma, human plasma transferrin and C3 complement were tested. Immunoblotting on agarose, compared with nitrocellulose, was quantitative and highly sensitive, with small amounts of protein (i.e., 100 pg) being detected. Moreover, albumin aggregates (i.e., dimer, trimer and tetramer) were blotted quantitatively in addition to the monomer, and their percentages were calculated. This method is sensitive, quantitative, reproducible, and includes fewer manipulations; furthermore, it is less expensive and does not require the use of toxic or carcinogenic agents.

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A simple and cheap remotely operated system for the iodination of proteins

Cited by 7 publications

References 1 publication

Two Cea and Three Nca Species, Although Distinguishable by Monoclonal Antibodies, Have Nearly Identical Peptide Patterns

Two Cea and Three Nca Species, Although Distinguishable by Monoclonal Antibodies, Have Nearly Identical Peptide Patterns

Pituitary responsiveness to synthetic LH-RH and pituitary LH content at various reproductive stages in the sheep

Electroblotting of proteins on agarose gel containing specific antibodies

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