Clinical Chemistry
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 30: 222-225, 1984;
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hiwada, K.
Right arrow Articles by Kokubu, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hiwada, K.
Right arrow Articles by Kokubu, T.

Clinical Chemistry, Vol 30, 222-225, Copyright © 1984 by American Association for Clinical Chemistry

A family with a high serum aminopeptidase (microsomal) activity: properties of the enzyme from serum of the propositus

K Hiwada, M Tokioka-Terao, K Nishimura and T Kokubu

We found a family with a high activity for hydrolyzing L-alanyl-beta- naphthylamide in their serum. This enzyme was confirmed to be aminopeptidase (microsomal) (EC 3.4.11.2) by means of immunological experiments involving anti-human kidney aminopeptidase (microsomal) antibody. We could not find the cause of the increased activity from the results of clinical and laboratory examinations. The enzyme from the propositus resembled that from the serum of normal subjects in molecular mass (240 000 Da), Km value (87 mumol/L), and degree of inhibition by antiserum to human kidney aminopeptidase (microsomal). It differed from the normal enzyme with respect to electrophoretic mobility (R1 value, 0.58; normal, 0.51), isoelectric point (pI, pH 3.4; normal, pH 3.8), and heat stability (more labile than normal). From information on this family and another one reported in the Japanese literature, we suggest that the mode of inheritance of a high activity of serum aminopeptidase (microsomal) may be autosomal dominant.


The following articles in journals at HighWire Press have cited this article:


Home page
 Clin. Chem.Home page
M. Kawai, Y. Hara, T. Kubota, K. Shiba, and S. Hosaki
A family with high serum leucine aminopeptidase activity derived from a novel variant CD13
Clin. Chem., February 1, 1998; 44(2): 215 - 220.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1984 by the American Association for Clinical Chemistry.