The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-α-trypsin inhibitor also encodes α-1-microgiobulin (protein HC (original) (raw)

Journal Article

,

Recombinant DNA-Chemistry, Microbiology Research, Biotechnology Group

PO Box 932, Miles Laboratories, Inc., Elkhart, IN 46515, USA

Search for other works by this author on:

,

Recombinant DNA-Chemistry, Microbiology Research, Biotechnology Group

PO Box 932, Miles Laboratories, Inc., Elkhart, IN 46515, USA

Search for other works by this author on:

Recombinant DNA-Chemistry, Microbiology Research, Biotechnology Group

PO Box 932, Miles Laboratories, Inc., Elkhart, IN 46515, USA

Search for other works by this author on:

Accepted:

15 September 1986

Published:

01 October 1986

• PDF
• Split View
• • Article contents
  • Figures & tables
  • Video
  • Audio
  • Supplementary Data
• Cite

Cite

John F. Kaumeyer, Joseph O. Polazzi, Michael P. Kotick, The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-α-trypsin inhibitor also encodes α-1-microgiobulin (protein HC, Nucleic Acids Research, Volume 14, Issue 20, 1 October 1986, Pages 7839–7850, https://doi.org/10.1093/nar/14.20.7839
Close

Navbar Search Filter Mobile Enter search term Search

Abstract

Inter-a-trypsin inhibitor (ITI) is a 180 kd serine proteinase inhibitor found in human serum. Treatment of 180 kd ITI with trypsin releases a 30 kd fragment (HI-30) which contains the anti-proteolytic activity of the high molecular weight form. We have isolated a cDNA clone from a human liver library which codes for HI-30, and have determined its DNA sequence. The mRNA not only codes for HI-30 but also another serum protein, α1-microglobulin, which has not been previously associated with ITI or HI-30. The α-1-microglobulin sequence is found in the amino-terminus of the protein and is preceded by a signal sequence. HI-30 is found at the carboxy-terminus. The two protein sequences are separated by two arginine residues.

This content is only available as a PDF.

© IRL Press Limited, Oxford, England

I agree to the terms and conditions. You must accept the terms and conditions.

Submit a comment

Name

Affiliations

Comment title

Comment

You have entered an invalid code

Thank you for submitting a comment on this article. Your comment will be reviewed and published at the journal's discretion. Please check for further notifications by email.

Citations

Views

Altmetric

Metrics

Total Views 80

15 Pageviews

65 PDF Downloads

Since 1/1/2017

Citations

220 Web of Science

×

Email alerts

Citing articles via

• Latest

• Most Read

• Most Cited

More from Oxford Academic