Development of monoclonal antibodies against creatine kinase MB2
Leickt, L ; Grubb, Anders LU
and Ohlson, S
(2002)
In Scandinavian Journal of Clinical & Laboratory Investigation
62(6).
p.423-429
- Abstract
- An increase of creatine kinase MB (CKMB) in serum has long been used as a marker for acute myocardial infarction (AMI). It is important with an early diagnosis and since the amount of the CKMB2 isoform rises above reference levels much earlier than the total creatine kinase amount, quantification of CKMB isoforms could be a feasible alternative for early analysis. The two CKMB isoforms differ by only one C-terminal lysine residue, which makes it difficult to separate one from the other. To overcome this problem, monoclonal antibodies were produced using unique peptides as antigen in hybridoma technology. Two peptides with 16 and 15 amino acids corresponding to the C-terminal end of the M-subunits of CKMB2 and CKMB1 respectively, were... (More)
- An increase of creatine kinase MB (CKMB) in serum has long been used as a marker for acute myocardial infarction (AMI). It is important with an early diagnosis and since the amount of the CKMB2 isoform rises above reference levels much earlier than the total creatine kinase amount, quantification of CKMB isoforms could be a feasible alternative for early analysis. The two CKMB isoforms differ by only one C-terminal lysine residue, which makes it difficult to separate one from the other. To overcome this problem, monoclonal antibodies were produced using unique peptides as antigen in hybridoma technology. Two peptides with 16 and 15 amino acids corresponding to the C-terminal end of the M-subunits of CKMB2 and CKMB1 respectively, were conjugated to keyhole limpet hemocyanin and used as antigens. Sixteen different monoclonal antibodies to these peptides were obtained and characterized. Their specificity was analyzed by immunoassay and 10 of the antibodies showed cross-reactive binding to creatine kinase. Surface plasmon resonance based biosensor analysis was used to determine affinity and kinetics towards the peptides and the epitopes of four of the antibodies were studied by means of phage display. Some of these antibodies have binding properties that might qualify them for use in the establishment of procedures allowing early diagnosis of AMI. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/322989
- author
- Leickt, L
; Grubb, Anders
LU
and Ohlson, S
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- acute myocardial infarction, CKMB2, peptide antigen
- in
- Scandinavian Journal of Clinical & Laboratory Investigation
- volume
- 62
- issue
- 6
- pages
- 423 - 429
- publisher
- Informa Healthcare
- external identifiers
-
- wos:000179228200003
- pmid:12469897
- scopus:0036428763
- ISSN
- 1502-7686
- DOI
- 10.1080/00365510260389976
- language
- English
- LU publication?
- yes
- id
- 5b4bdcb1-ed2e-4c2c-a55e-69c41b800501 (old id 322989)
- date added to LUP
- 2016-04-01 17:09:07
- date last changed
- 2023-01-05 05:35:17
@article{5b4bdcb1-ed2e-4c2c-a55e-69c41b800501,
abstract = {{An increase of creatine kinase MB (CKMB) in serum has long been used as a marker for acute myocardial infarction (AMI). It is important with an early diagnosis and since the amount of the CKMB2 isoform rises above reference levels much earlier than the total creatine kinase amount, quantification of CKMB isoforms could be a feasible alternative for early analysis. The two CKMB isoforms differ by only one C-terminal lysine residue, which makes it difficult to separate one from the other. To overcome this problem, monoclonal antibodies were produced using unique peptides as antigen in hybridoma technology. Two peptides with 16 and 15 amino acids corresponding to the C-terminal end of the M-subunits of CKMB2 and CKMB1 respectively, were conjugated to keyhole limpet hemocyanin and used as antigens. Sixteen different monoclonal antibodies to these peptides were obtained and characterized. Their specificity was analyzed by immunoassay and 10 of the antibodies showed cross-reactive binding to creatine kinase. Surface plasmon resonance based biosensor analysis was used to determine affinity and kinetics towards the peptides and the epitopes of four of the antibodies were studied by means of phage display. Some of these antibodies have binding properties that might qualify them for use in the establishment of procedures allowing early diagnosis of AMI.}},
author = {{Leickt, L and Grubb, Anders and Ohlson, S}},
issn = {{1502-7686}},
keywords = {{acute myocardial infarction; CKMB2; peptide antigen}},
language = {{eng}},
number = {{6}},
pages = {{423--429}},
publisher = {{Informa Healthcare}},
series = {{Scandinavian Journal of Clinical & Laboratory Investigation}},
title = {{Development of monoclonal antibodies against creatine kinase MB2}},
url = {{http://dx.doi.org/10.1080/00365510260389976}},
doi = {{10.1080/00365510260389976}},
volume = {{62}},
year = {{2002}},
}