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 KOMIYA, M.
Right arrow Articles by SUZUKI, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by KOMIYA, M.
Right arrow Articles by SUZUKI, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1974, Vol. 76, No. 4 823-832
© 1974 Japanese Biochemical Society

research-article

Bovine Plasma Kininogens

II. Microheterogeneities of High Molecular Weight Kininogens and Their Structural Relationships

Masanobu KOMIYA, Hisao KATO and Tomoji SUZUKI

Division of Plasma Proteins, Institute for Protein Research, Osaka University Suita, Osaka 565

As described in the preceding paper, a high molecular weight (HMW) kininogen purified from fresh bovine plasma contained two components, kininogen-a and -b, which were susceptible to plasma kallikrein [EC 3.4.21.8 [EC] ]. These components were partially separated by ion exchange chromatography on a long column of CM-Sephadex C-50. They had the same molecular weight of about 8.0×104 and their amino acid compositions and tryptic peptide maps were indistinguishable. Thus, these two kininogens seem to be essentially the same molecular species. The difference between them was found to be due to a few peptide bond cleavages along the polypeptide chain of the kininogen molecule. Evidence for this was as follows:

  1. The molecular weight of kininogen-b did not change after cleavage of disulfide bridges, while that of kininogen-a clearly decreased after reduction.
  2. The theoretical amount of N-terminal amino acid could not be recovered from HMW kininogens, suggesting that the N-terminal amino acid was in a masked form. However, careful analysis by the dinitrofluorobenzene method indicated the presence of 0.2 mole of serine per mole of protein. On hydrazinolysis of the HMW kininogens, leucine was identified as the C-terminal residue. Treatment of the proteins with carboxypeptidase A [EC 3.4.12.2 [EC] [EC] ] and B [EC 3.4.12.3 [EC] [EC] ] liberated one mole of leucine and 0.3 mole of arginine per mole of protein.
  3. On treatment of HMW kininogen-a and -b with cyanogen bromide (CNBr), the former yielded kallidin in addition to a fragment from which kallidin was liberated by trypsin, while the latter yielded only the fragment containing kallidin.

On the basis of the above results, it was concluded that kininogen-b consists of a single intact polypeptide chain with a masked N-terminal and with C-terminal leucine, while kininogen-a consists of two proteins, one with a kinin moiety at the C-terminus and the other with this moiety in the interior. These microheterogeneous kininogens are thought to be derived from kininogen-b by cleavage of a few peptide bonds within polypeptide chains bridged through a disulfide linkage.


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 BiochemHome page
J.-i. Yamamura, Y. Morita, Y. Takada, and H. Kawakami
The Fragments of Bovine High Molecular Weight Kininogen Promote Osteoblast Proliferation In Vitro
J. Biochem., December 1, 2006; 140(6): 825 - 830.
[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.