Proteolytic specificity of elastase on bovine αs1-casein
49
Citation
53
Reference
10
Related Paper
Citation Trend
Keywords:
Proteolysis
Cleavage (geology)
Phosphate buffered saline
Summary The effect of human granulocyte proteases and related pancreatic enzymes on the procoagulant (VIII:C) and the von Willebrand (VIIIR:WF) activities of factor VIII was investigated. VIII:C appeared to be several hundred times more sensitive towards granulocyte enzymes than VIIIR: WF. The elastase-like protease (ELP) decreased both activities of factor VIII more effectively than the chymotrypsin-like enzyme (CLP). ELP increased co-operatively the inactivating effect of CLP. In the presence of a CLP-ELP mixture in a ratio of 3:1, the rate of inactivation of VIII:C was seven times as high as that with CLP alone. Factor VIII was more resistant towards the damaging effect of pancreatic enzymes. The rate of inactivation of VIII: C was about a thousand times and that of VIIIR:WF about a hundred times lower than those measured with the related granulocyte enzymes of the same proteolytic activity. The sensitivity of VIII: C towards proteolysis was not as pronounced with pancreatic enzymes as with granulocyte proteases. Our data suggest that, even though CLP and ELP are called "-like" enzymes, the specificity of granulocyte proteases is not identical with that of the pancreatic enzymes. The extreme sensitivity of VIII: C for granulocyte proteases may bring about blood coagulation disorders in certain pathological conditions.
Proteolysis
Pancreatic elastase
Cite
Citations (26)
Proteolysis
Neutrophil elastase
Cite
Citations (22)
Proteolysis
Bovine milk
Proteolytic enzymes
Digestion
Milk protein
Exopeptidase
Cite
Citations (40)
Abstract The stability of the neutral and alkaline proteases in a Bacillus subtilis enzyme mixture was studied in aqueous solutions at room temperature. Stabilization of the proteases in solution for periods up to 25 days was achieved by the addition of various protein preparations including casein and soya protein. The degree of stabilization by casein was concentration dependent to about 2% protein. The instability of the neutral protease in solutions of the B. subtilis enzyme mixture was shown to be due primarily to proteolysis by the alkaline protease since the diisopropylfluorophosphate‐treated enzyme was quite stable. Formulation of such enzyme solutions at low pH gave greater stability as did solutions containing an alkaline protease inhibitor from potatoes. A Conceptual approach to the formulation of enzyme solutions containing proteolytic enzyme to ensure maximum stability is proposed.
Proteolysis
Alkaline protease
Proteolytic enzymes
Neutral protease
Cite
Citations (12)
Subtilisin
Serine Proteinase Inhibitors
Proteolysis
Trypsin inhibitor
Proteolytic enzymes
Proteinase 3
Pancreatic elastase
Proteinase inhibitor
Cite
Citations (13)
A protein resistant to heat and proteolysis that inhibits serine proteases was isolated from wheat leaf apoplasts. Based on trypsin inhibition, its more active form was a 66–69 kDa oligomer. It was dissociated in an 18–21 kDa monomer having an amino terminal sequence identical to the Box A of germins and germin‐like proteins. Like these proteins, it was glycosylated and showed manganese superoxide dismutase activity. The monomer displayed three forms when examined by 2D western blot: two of 19 kDa, pI 5.8 and 6.2; and one of 21 kDa, pI 5.8. It was found that the protein controls serine protease activity in the apoplast of plants challenged with the fungus Septoria tritici.
Proteolysis
Cite
Citations (64)
Cleavage (geology)
Proteolysis
Cite
Citations (17)
Proteolysis
Cite
Citations (2)
Proteolysis
Pulmonary emphysema
Pancreatic elastase
Cite
Citations (8)
Commercial proteases suitable for soymilk-curd production by limited proteolysis with immobilized enzyme reactor were selected from three plant and a microbial proteases. Limited proteolysis of soy-protein with the enzymes at 30, 5 and 0°C was examined by an electrophoresis. Two commercial preparations of papain and a preparation of bromelain, which were plant proteases, limitedly digested native soyprotein even under the low temperature conditions. The soy-protein solution and soymilk treated with the plant proteases at 5°C gave curd by heat treatment. The plant enzymes were immobilized on SP-Sephadex C-25. The immobilized enzymes digested the soy-protein similarly to the free enzymes. Soymilk-curd was also obtained from the soymilk hydrolyzed with the immobilized enzymes.
Proteolysis
Bromelain
Proteolytic enzymes
Sephadex
Cite
Citations (6)