Human plasma carboxypeptidase B

• US 5,206,161 A
• Filed: 02/01/1991
• Issued: 04/27/1993
• Est. Priority Date: 02/01/1991
• Status: Expired due to Term

• Current Assignee: Genentech, Inc. (Roche Holding AG)
• Original Assignee: Genentech, Inc. (Roche Holding AG)
• Inventors: Eaton, Dan L., Drayna, Dennis T.
• Primary Examiner(s): Naff, David M.
• Assistant Examiner(s): WEBER, JON P
• Application Number:
  US07/649,591
• Time in Patent Office: 816 Days
• Field of Search: 435/212
• US Class Current: 435/212
• CPC Class Codes: A61K 38/00 Medicinal preparations containing peptides peptides containing beta-lactam rings A61K31/00; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, A61K31/00; ergot alkaloids of the cyclic peptide type A61K31/48; containing macromolecular compounds having statistically distributed amino acid units A61K31/74; medicinal preparations containing antigens or antibodies A61K39/00; medicinal preparations characterised by the non-active ingredients, e.g. peptides as drug carriers, A61K47/00
• CPC Class Codes: C12N 9/48 acting on peptide bonds (3.4)
• CPC Class Codes: G01N 33/573 for enzymes or isoenzymes
• CPC Class Codes: Y10S 436/824 Immunological separation techniques

Abstract

A novel polypeptide, designated plasma carboxypeptidase B (PCPB), has been purified from human plasma. It has been cloned from a human liver cDNA library using PCR amplification. Provided herein is nucleic acid encoding PCPB useful in diagnostics and in the recombinant preparation of PCPB. PCPB is used in the preparation and purification of antibodies thereto, in the purification of plasminogen, in the inhibition of plasminogen activation by t-PA in the presence of fibrinogen, and in diagnostic assays.

Claims

1. An isolated monomeric human plasma carboxypeptidase B (PCPB) having a molecular weight on non-reducing SDS-PAGE of about 60 kD and having in its mature form the N-terminal sequence PheGluSer.

2. The PCPB of claim 1 constituting the amino acid sequence shown in FIG. 4 beginning at the mature N-terminus.

3. The PCPB of claim 1 constituting an activation peptide fragment having the amino acid sequence shown in FIG. 4 beginning at the phenylalanine at the mature N-terminus and ending at the arginine at position 92.

4. The PCPB of claim 1 constituting a carboxypeptidase-active fragment having the amino acid sequence shown in FIG. 4 beginning at the alanine at position 93 and ending at the valine at position 401.