Monoclonal antibodies to hydroxyindole -methyltransferase from bovine pineal gland

Deguchi, Takao; Yokoyama, Emiko; Ichikawa, Tomoyuki

doi:10.1016/s0006-8993(87)80001-x

Cited by 2 publications

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“…In contrast, no reactive band was demonstrated in the crude supernatant (lanes 1, 3, and 5), indicating that the content of ChAT in the crude supernatant was too low to detect by the present method. The control blot using antibovine HIOMT-717 (Deguchi et al, 1987) did not stain any proteins in both ChAT preparations, but stained HIOMT protein (38 kDa) in bovine pineal supernatant (Fig. 3, lane 9).…”

Section: Immunoblot Analysismentioning

confidence: 93%

“…ChAT activity in the supernatant decreased only when the enzyme- antibody complex was removed by precipitation with anti-mouse IgG coupled to IgG sorb. Control incubation using anti-bovine hydroxyindole O-methyltransferase (HIOMT) monoclonal antibodies (Deguchi et al, 1987) did not react with ChAT. The results indicated that the anti-bovine ChAT antibodies reacted with the enzyme without blocking the catalytic site.…”

Section: Production Of Anti-bovine Chat Monoclonal Antibodiesmentioning

confidence: 99%

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Monoclonal Antibodies to and Immunoaffinity Purification of Choline Acetyltransferase from Bovine Brain

Ichikawa¹,

Deguchi

1987

Journal of Neurochemistry

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Three hybridomas producing monoclonal antibodies to bovine brain choline acetyltransferase (ChAT) have been established by fusion of the spleen cells from a mouse immunized with purified enzyme with myeloma NS-1 cells. All three clones produced IgGl antibodies that reacted with enzyme protein denatured with sodium dodecyl sulfate. By using one of the monoclonal antibodies, a rapid and efficient immunoaffinity purification procedure of bovine ChAT has been established. Immunoblot analysis and immunoaffinity purification indicated that bovine ChAT is a single 68-kilodalton protein. The monoclonal antibodies will offer us a good tool to isolate the cDNA clones encoding ChAT.

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Section: Immunoblot Analysismentioning

confidence: 93%

Section: Production Of Anti-bovine Chat Monoclonal Antibodiesmentioning

confidence: 99%

Monoclonal Antibodies to and Immunoaffinity Purification of Choline Acetyltransferase from Bovine Brain

Ichikawa¹,

Deguchi

1987

Journal of Neurochemistry

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Localization of hydroxyindole O-methyltransferase-synthesizing cells in bovine epithalamus: immunocytochemistry and in-situ hybridization

Sato

Deguchi

Ichikawa³

et al. 1991

Cell Tissue Res

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Hydroxyindole O-methyltransferase (HIOMT)-immunoreactive cells and melatonin synthesis were demonstrated in bovine epithalamus (including the pineal gland) with monoclonal antibodies and cRNA probes to HIOMT. The HIOMT-immunoreactive product was present in the cytoplasm of pinealocytes. All identifiable pinealocytes were clearly labeled in the pineal gland. The expression of the HIOMT gene was first identified in pinealocyte cytoplasm by in-situ hybridization (ISH). The distribution of the hybridization-positive cells in the pineal gland was compatible with that revealed by immunocytochemistry using the monoclonal antibody to HIOMT. In addition, HIOMT transcripts were found in the medial habenular nucleus, and the habenular and posterior commissure; they may correspond to S-antigen-immunoreactive cells demonstrated in the same regions of the hamster and the mouse. In these regions, the hybridization-positive cells did not exhibit HIOMT-immunoreactivity; thus, cells devoid of immunoreactivity may synthesize but rapidly transport the newly synthesized proteins. These results indicate (1) that the conversion of N-acetylserotonin into melatonin takes place in the cytoplasm of pinealocytes, (2) that some epithalamic cells in the habenular area may synthesize melatonin, and (3) that melatonin may act as a chemical messenger in centrally directed processes, as shown by using S-antigen immunocytochemistry.

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Monoclonal antibodies to hydroxyindole -methyltransferase from bovine pineal gland

Cited by 2 publications

References 0 publications

Monoclonal Antibodies to and Immunoaffinity Purification of Choline Acetyltransferase from Bovine Brain

Monoclonal Antibodies to and Immunoaffinity Purification of Choline Acetyltransferase from Bovine Brain

Localization of hydroxyindole O-methyltransferase-synthesizing cells in bovine epithalamus: immunocytochemistry and in-situ hybridization

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