PMID- 2968815
OWN - NLM
STAT- MEDLINE
DCOM- 19880817
LR  - 20190609
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 966
IP  - 1
DP  - 1988 Jul 14
TI  - Acid-stable trypsin-plasmin inhibitors formed enzymatically from plasma precursor 
      protein.
PG  - 1-11
AB  - Enzymatic formation of acid-stable trypsin-plasmin inhibitors (ASTPIs) in human 
      plasma with several proteinases, particularly SH-proteinases, was demonstrated. 
      The maximal activity obtained with bromelain was 40 U/ml plasma, which 
      corresponded to about a 10-fold increase as compared to the untreated control 
      plasma (4.2 U/ml). Gel filtration revealed at least two ASTPI activity peaks of 
      molecular weight 16,000 (main peak) and 8000 (minor peak). The main ASTPI was 
      further purified by trypsin-Sepharose affinity chromatography, isoelectric 
      focusing and gel filtration on Sephadex G-75 superfine. The purified inhibitor 
      was found to be identical to the active fragment of plasma ASTPI or urinary 
      trypsin inhibitor (UTI) formed by bromelain treatment. It had an isoelectric 
      point (pI) of 3.7, a molecular weight of 16,000 by SDS-polyacrylamide gel 
      electrophoresis and was a glycine- and glutamic acid-rich protein lacking 
      histidine. The NH2-terminal amino acid sequence was 
      H2N-(Lys)-Glu-Asp-Ser-X-Gln-Leu-Gly-Tyr-Ser-Ala-Gly-Pro-X-Met-Gly-Met-Th r-X-Arg 
      - Tyr-Phe-Tyr-... COOH, which was homologous to the Lys22-Met36 part (or 
      Glu23-Met36 part; 30% of the total) of the plasma ASTPI or UTI molecule 
      (molecular weight 70,000-80,000 by gel filtration). The purified ASTPI displayed 
      the same antigenicity as UTI and exerted strong inhibitory effects on trypsin, 
      chymotrypsin and plasmin amidolysis, but had a much lesser effect on plasmin 
      fibrinolysis. It also strongly inhibited non-plasmic fibrinolysis with human 
      leukocyte proteinase and earthworm proteinase.
FAU - Sumi, H
AU  - Sumi H
AD  - Department of Physiology, Miyazaki Medical College, Okayama, Japan.
FAU - Yoshida, E
AU  - Yoshida E
FAU - Hamada, H
AU  - Hamada H
FAU - Mihara, H
AU  - Mihara H
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Blood Proteins)
RN  - 0 (Protein Precursors)
RN  - 0 (Trypsin Inhibitors)
RN  - EC 3.4.- (Peptide Hydrolases)
RN  - EC 3.4.21.7 (Fibrinolysin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Blood Proteins/metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Fibrinolysin/antagonists & inhibitors/*isolation & purification/metabolism
MH  - Fibrinolysis
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Immunodiffusion
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Peptide Hydrolases/metabolism
MH  - Protein Precursors/metabolism
MH  - Trypsin Inhibitors/*isolation & purification
EDAT- 1988/07/14 00:00
MHDA- 1988/07/14 00:01
CRDT- 1988/07/14 00:00
PHST- 1988/07/14 00:00 [pubmed]
PHST- 1988/07/14 00:01 [medline]
PHST- 1988/07/14 00:00 [entrez]
AID - 0304-4165(88)90122-5 [pii]
AID - 10.1016/0304-4165(88)90122-5 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1988 Jul 14;966(1):1-11. doi: 10.1016/0304-4165(88)90122-5.