Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by KOMINAMI, E.
Right arrow Articles by KATUNUMA, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by KOMINAMI, E.
Right arrow Articles by KATUNUMA, N.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1984, Vol. 96, No. 5 1437-1442
© 1984 Japanese Biochemical Society

research-article

Different Tissue Distributions of Two Types of Thiol Proteinase Inhibitors from Rat Liver and Epidermis1

Eiki KOMINAMI, Yoshiaki BANDO, Nobuaki WAKAMATSU and Nobuhiko KATUNUMA

Department of Enzyme Chemistry, Institute for Enzyme Research, School of Medicine, The University of Tokushima Tokushima, Tokushima 770

The concentrations of two types of endogenous inhibitors of thiol proteinases were determined in soluble extracts of various rat tissues by means of a sensitive enzyme immunoassay method, which consisted of solid-phase immobilized anti-rat liver inhibitor or anti-rat epidermal inhibitor and antibodies labeled with horseradish peroxidase. The minimum detectable amounts of inhibitors from liver and epidermis were 30 pg and 3 pg/assay, respectively. The tissue distributions of the epidermal and liver-type inhibitors were found to differ. The liver-type inhibitor was found to be widely distributed in various tissues at levels of 76–420 ng/mg protein, whereas the epidermal-type inhibitor was found at high levels in the skin, tongue, esophagus, stomach, intestine, and vagina, but at quite low levels in other tissues tested.

1 This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan, grants from the National Center of Nervous, Mental and Muscular Disorders of the Ministry of Health and Welfare of Japan, and grants from the Japanese Foundation of Metabolism and Diseases, the Naito Foundation, and the Japanese Foundation of Applied Enzymology.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Gen. Virol.Home page
P. Peri, V. Hukkanen, K. Nuutila, P. Saukko, M. Abrahamson, and T. Vuorinen
The cysteine protease inhibitors cystatins inhibit herpes simplex virus type 1-induced apoptosis and virus yield in HEp-2 cells
J. Gen. Virol., August 1, 2007; 88(8): 2101 - 2105.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Pathol.Home page
T Leinonen, R Pirinen, J Bohm, R Johansson, A Rinne, E Weber, and V-M Kosma
Biological and prognostic role of acid cysteine proteinase inhibitor (ACPI, cystatin A) in non-small-cell lung cancer
J. Clin. Pathol., May 1, 2007; 60(5): 515 - 519.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
B. Jones, P. J. Roberts, W. A. Faubion, E. Kominami, and G. J. Gores
Cystatin A expression reduces bile salt-induced apoptosis in a rat hepatoma cell line
Am J Physiol Gastrointest Liver Physiol, October 1, 1998; 275(4): G723 - G730.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.