Preparation of 125I-protein A usable for up to 10 months in immunoassays

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Standard

Preparation of 125I-protein A usable for up to 10 months in immunoassays. / Dyrberg, T; Billestrup, Nils.

I: Journal of Immunological Methods, Bind 71, Nr. 2, 06.07.1984, s. 193-201.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Dyrberg, T & Billestrup, N 1984, 'Preparation of 125I-protein A usable for up to 10 months in immunoassays', Journal of Immunological Methods, bind 71, nr. 2, s. 193-201.

APA

Dyrberg, T., & Billestrup, N. (1984). Preparation of 125I-protein A usable for up to 10 months in immunoassays. Journal of Immunological Methods, 71(2), 193-201.

Vancouver

Dyrberg T, Billestrup N. Preparation of 125I-protein A usable for up to 10 months in immunoassays. Journal of Immunological Methods. 1984 jul. 6;71(2):193-201.

Author

Dyrberg, T ; Billestrup, Nils. / Preparation of 125I-protein A usable for up to 10 months in immunoassays. I: Journal of Immunological Methods. 1984 ; Bind 71, Nr. 2. s. 193-201.

Bibtex

@article{ff5c5a871cb7488a8a69210802027a38,
title = "Preparation of 125I-protein A usable for up to 10 months in immunoassays",
abstract = "Chloramine-T iodination of protein A from Staphylococcus aureus and gel electrophoretic purification of the iodination mixture results in a stable tracer of high specific and functional activity. Following repeated gel electrophoresis of the tracer only a single component was observed. The specific activity of the 125I-protein A was between 30 and 55 muCi/micrograms. The binding of 125I-protein A to rabbit immunoglobulin exceeded 90% and the tracer competed effectively with unlabelled protein A in binding to cells incubated with sera containing surface antibodies. Storage of the tracer for up to 46 weeks resulted in a moderate decrease in maximal binding to immunoglobulin (from 91% to 64%), in TCA precipitable radioactivity (from 97% to 80%) and an approx. 30% decrease in the ability to detect cell bound immunoglobulin. It is concluded that gel electrophoretic purification of 125I-protein A produces a tracer with a very long shelf life.",
keywords = "Chloramines, Electrophoresis, Polyacrylamide Gel, Iodine Radioisotopes, Isotope Labeling, Staphylococcal Protein A, Tosyl Compounds",
author = "T Dyrberg and Nils Billestrup",
year = "1984",
month = jul,
day = "6",
language = "English",
volume = "71",
pages = "193--201",
journal = "Journal of Immunological Methods",
issn = "0022-1759",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Preparation of 125I-protein A usable for up to 10 months in immunoassays

AU - Dyrberg, T

AU - Billestrup, Nils

PY - 1984/7/6

Y1 - 1984/7/6

N2 - Chloramine-T iodination of protein A from Staphylococcus aureus and gel electrophoretic purification of the iodination mixture results in a stable tracer of high specific and functional activity. Following repeated gel electrophoresis of the tracer only a single component was observed. The specific activity of the 125I-protein A was between 30 and 55 muCi/micrograms. The binding of 125I-protein A to rabbit immunoglobulin exceeded 90% and the tracer competed effectively with unlabelled protein A in binding to cells incubated with sera containing surface antibodies. Storage of the tracer for up to 46 weeks resulted in a moderate decrease in maximal binding to immunoglobulin (from 91% to 64%), in TCA precipitable radioactivity (from 97% to 80%) and an approx. 30% decrease in the ability to detect cell bound immunoglobulin. It is concluded that gel electrophoretic purification of 125I-protein A produces a tracer with a very long shelf life.

AB - Chloramine-T iodination of protein A from Staphylococcus aureus and gel electrophoretic purification of the iodination mixture results in a stable tracer of high specific and functional activity. Following repeated gel electrophoresis of the tracer only a single component was observed. The specific activity of the 125I-protein A was between 30 and 55 muCi/micrograms. The binding of 125I-protein A to rabbit immunoglobulin exceeded 90% and the tracer competed effectively with unlabelled protein A in binding to cells incubated with sera containing surface antibodies. Storage of the tracer for up to 46 weeks resulted in a moderate decrease in maximal binding to immunoglobulin (from 91% to 64%), in TCA precipitable radioactivity (from 97% to 80%) and an approx. 30% decrease in the ability to detect cell bound immunoglobulin. It is concluded that gel electrophoretic purification of 125I-protein A produces a tracer with a very long shelf life.

KW - Chloramines

KW - Electrophoresis, Polyacrylamide Gel

KW - Iodine Radioisotopes

KW - Isotope Labeling

KW - Staphylococcal Protein A

KW - Tosyl Compounds

M3 - Journal article

C2 - 6736658

VL - 71

SP - 193

EP - 201

JO - Journal of Immunological Methods

JF - Journal of Immunological Methods

SN - 0022-1759

IS - 2

ER -

ID: 132900976