Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. 2. Limited proteolysis of Curcurbita maxima trypsin inhibitor I by pepsin

Biochemistry ◽  
1994 ◽  
Vol 33 (1) ◽  
pp. 208-213 ◽  
Author(s):  
Jacek Otlewski ◽  
Tomasz Zbyryt ◽  
Marek Dryjanski ◽  
Grzegorz Bulaj ◽  
Tadeusz Wilusz
Keyword(s):  
Trypsin Inhibitor ◽  
Limited Proteolysis ◽  
Peptide Bond ◽  
Serine Proteinases ◽  
Single Peptide

Binding of the kunitz-type trypsin inhibitor DE-3 fromErythrina caffra seeds to serine proteinases: a comparative study

1992 ◽  
Vol 5 (3) ◽  
pp. 105-114 ◽  
Author(s):  
Silvia Onesti ◽  
David J. Matthews ◽  
Patrizia Aducci ◽  
Gino Amiconi ◽  
Martino Bolognesi ◽  
...  
Keyword(s):  
Comparative Study ◽  
Trypsin Inhibitor ◽  
Serine Proteinases ◽  
Kunitz Type

scholarly journals Reaction of a tumour-associated trypsin inhibitor with serine proteinases associated with coagulation and tumour invasion

1988 ◽  
Vol 254 (3) ◽  
pp. 911-914 ◽  
Author(s):  
U Turpeinen ◽  
E Koivunen ◽  
U H Stenman
Keyword(s):  
Plasminogen Activator ◽  
Tissue Plasminogen Activator ◽  
Trypsin Inhibitor ◽  
Synthetic Peptide ◽  
Serine Proteinases ◽  
Tumour Invasion ◽  
Peptide Substrates ◽  
Tissue Plasminogen

The inhibition of six serine proteinases by a tumour-associated trypsin inhibitor (TATI) was studied using synthetic peptide substrates. Physiological concentrations of TATI inhibited the amidolytic activities of trypsin, plasmin, urokinase and tissue plasminogen activator (tPA). Chymotrypsin, kallikrein and thrombin were also inhibited, but by much higher concentrations of TATI. The ability of TATI to inhibit trypsin, plasmin, urokinase and tPA suggests that it has a role in proteolytic processes in vivo involving these enzymes.

scholarly journals Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide

1991 ◽  
Vol 277 (3) ◽  
pp. 631-634 ◽  
Author(s):  
A R Hayman ◽  
A J Dryden ◽  
T J Chambers ◽  
M J Warburton
Keyword(s):  
Acid Phosphatase ◽  
Peptide Bond ◽  
Northern Blotting ◽  
Tartrate Resistant Acid Phosphatase ◽  
Acid Phosphatases ◽  
Post Translational Modification ◽  
Subunit Protein ◽  
Single Polypeptide ◽  
Single Peptide

Tartrate-resistant acid phosphatases have been isolated from a number of sources. These enzymes consist of one subunit (Mr 30,000-40,000) or two dissimilar subunits (Mr 15,000-20,000). Previously we isolated the enzyme from human osteoclastomas, as a two-subunit protein. By Northern blotting and hybridization with radiolabelled oligonucleotides corresponding to the N-terminal sequences of the two subunits, we demonstrate here that the enzyme is transcribed as one mRNA which is translated in vitro to produce a single polypeptide of approx. Mr 33,000. Transcription as a single mRNA species is also the case in other tissues. These results suggest that the osteoclastoma enzyme undergoes post-translational modification in the form of cleavage of a single peptide bond to give a disulphide-bonded two-subunit protein.

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