Chemistry: analytical and immunological testing – Involving an insoluble carrier for immobilizing immunochemicals
Patent
1986-09-24
1989-01-10
Warden, Robert J.
Chemistry: analytical and immunological testing
Involving an insoluble carrier for immobilizing immunochemicals
4351722, 43524027, 435948, 436536, 436543, 436547, 436548, 436815, 436822, 530387, 530807, 530808, 935110, G01N 33531, G01N 33532, G01N 33543, G01N 33577
Patent
active
047973706
DESCRIPTION:
BRIEF SUMMARY
The preparation of this invention contains antigen-binding entities i.e. intact antibodies or their antigen-binding fragments or derivatives which are directed against at least one structural element in 4-(2-aminoethyl)imidazolyl. This will thus also imply an antibody activity against histamine and/or against some of the biological degradation products of histamine, in particular 1-methyl-4-(2-aminoethyl)imidazole (=methyl histamine).
When the terms "antibody(ies)" or "antigen binding entity(ies)" are used with reference to the invention, they mean the antibody preparation as such--not the different antigen binding entities that may exist in the preparation.
Very little has been published concerning antibodies possessing specificity for methyl histamine, the reason being presumably that methyl histamine is not considered to be of the same crucial importance biologically as is histamine. Recently however it has been pointed out that quantification of methyl histamine might give potential advantages.
Previously known histamine antibody preparations have all been of poor quality. As a rule their affinity or specificity properties have been inadequate; for example, cross reactivity with other related compounds encountered in vivo has been unacceptably high. One such related compound is histidine which has a natural in vivo concentration more than 1,000 times higher than that of histamine.
U.S. Pat. Nos. 2,301,532, 2,372,066, 3,873,697, Chemical Abstracts 42 (1948) p. 3062-63 (i and a resp.), Agents and Actions 14 (1984) p. 574-79, and Proc. Natl. Acad. Sci. U.S.A. 81 (1984) p. 2572-76 describe the use of various immunogens containing histamine covalently bound to a carrier in essentially two different modes. One of these binding modes utilizes the primary amino group either in an amidated form or directly bound to an azo group. According to the other mode of binding, one position of the histamine imidazole ring is directly bound to an azo, carbonyl or phenyl group. Binding to the primary amino group involves elimination of the structural feature that distinguishes histamine and histidine from each other; such immunogens have been found to be poor in quality. Introduction of an azo, carbonyl or phenyl group on an atom of the imidazole ring involves a major disturbance of the ring electron configuration, which in turn means that the similarity to histamine is largely lost: This perhaps is why such immunogens have never produced antibodies showing any significant degree of specificity for histamine.
Neuroscience Letters 29 (1982) p. 105-06 describes the production of a non-covalent complex of histamine and methylated BSA (bovine serum albumin) and the use of that complex for producing an antiserum to histamine.
U.S. Pat. Nos. 3,759,890 and 4,016,146 ring derivatization of imidazole ring and the benzene ring of phenethylamines are described. None of the products obtained exhibits an aliphatically bound 4-(2-aminoethyl)imidazolyl group.
In a lecture (J. All. Clin. Immunol. 71 (1983) suppl. p. 152) antibodies have been described which are directed against histamine and are said to be exempt from cross recctivity with histidine. They have been employed in an immunological assay procedure.
EP-A No. 110,640 describes a histamine assay method employing histamine receptors from a T-lymphoblastoid cell line.
The antibodies of this invention are to be employed primarily in various immunological assay methods. This however does not in any way exclude the possibility that the antibodies of this invention may also be useful in other fields. Satisfactory immunological assay methods for methyl histamine and/or histamine are quite rare, presumably because no antibody preparations which are good enough for this purpose are available. Histamine determinations have usually been made by employing other techniques, all of which have been cumbersome and time-consuming.
Clinical fields in which histamine determinations have to be made comprise all types of conditions that involve an increased release of histamine, for example in any of
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Akerblom Eva B.
Berglund Asta B.
Hedin Anders J.
Pharmacia AB
Philpitt Fred
Saunders David A.
Warden Robert J.
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