Detection of light signals by microencapsulated cis-cinnamoyl chymotrypsin

Березин, И.В.; Kazanskaya, N.F.; Айсина, Р.Б.; Лукашева, Е. В.

doi:10.1016/0141-0229(80)90072-1

Cited by 4 publications

(4 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, it was concluded that staining can be attributed only to protein. Further, indoxyl ester was used for visualization of the encapsulated esterase-chymotrypsin as it was proposed earlier (Berezin et al, 1980). The product of indoxyl butyrate hydrolysis-indoxyl was then oxidized to bright blue indigo.…”

Section: Encapsulation Efficiency and Visualization Of Encapsulated Ementioning

confidence: 99%

Encapsulation of proteins by layer‐by‐layer adsorption of polyelectrolytes onto protein aggregates: Factors regulating the protein release

Balabushevitch

Sukhorukov

Moroz

et al. 2001

Biotech & Bioengineering

138

View full text Add to dashboard Cite

A novel method of protein encapsulation is proposed. Preformed protein aggregates are covered with polyelectrolyte layers by means of layer-by-layer adsorption. The polyelectrolyte membrane prevents protein leakage out of the capsule. Using chymotrypsin as a model enzyme the capsule wall selective permeability was demonstrated for substrates and inhibitors of different molecular weight and solubility.

show abstract

Section: Encapsulation Efficiency and Visualization Of Encapsulated Ementioning

confidence: 99%

Encapsulation of proteins by layer‐by‐layer adsorption of polyelectrolytes onto protein aggregates: Factors regulating the protein release

Balabushevitch

Sukhorukov

Moroz

et al. 2001

Biotech & Bioengineering

138

View full text Add to dashboard Cite

show abstract

“…This is confirmed by the fact that most of the work with inhibited a-CT has been done through acylation with cis-CI. [12][13][14]22 …”

Section: Resultsmentioning

confidence: 99%

“…The p-nitrophenyl-&(Ipyrenyll-acrylate had an overall yield of 63%; the melting point was 184°C. Also, rnle = 394(7), 393 (22), 364(1), 348( I), 271( I), and 255( 100). The p-nitrophenyl-P-( Inaphthy1)-acrylate had an overall yield of 62%; the melting point was 138°C.…”

Section: Preparation Of N-(/3-aryl-propenoyl)imidazole Derivativesmentioning

confidence: 97%

Inhibition or initiation of a radical polymerization reaction by an ultraviolet‐induced enzymatic process

Deynse

Desie

Schryver

et al. 1987

Biotech & Bioengineering

View full text Add to dashboard Cite

alpha-Chymotrypsin was modified to a light-controllable enzyme derivative by acylating active serine 195 residue with a cinnamoyl group or analogue. Upon UV irradiation the acylgroup could be isomerized, leading to release of the inhibiting group. Enzymatic activity could thus be regulated by means of UV light. A full 100% inhibition of the enzymatic activity could not be reached by the cinnamoyl derivative. Only posttreatment with diisopropylfluorophosphate yields a fully inactive enzyme derivative. The shelf-life of the inhibited enzyme was rather poor. Only freeze-dried samples could be used for several months without significant recovery of activity. Adapting the sensitivity of the system to visible light seems limited to the size of an enzyme's active site. Combination of the enzymatic system producing an inhibitor or an initiator with a polymerization reaction can result in a photographic process with a higher amplification factor.

show abstract

“…Several approaches have been taken to develop strategies for photo-control of enzyme catalytic activity. These approaches include: (1) control of p H and consequently enzyme activity by light; ( 2 ) control of the concentration of a coenzyme or critical cofactor by light; (3) control of the concentration of an enzyme competitive inhibitor by light; (4) control of the concentration of an irreversible enzyme inhibitor by light, and ( 5 ) modification of an enzyme with a photosensitive group that can be removed by light (Martinek et a/., 1971;Berezin et a / . , 1980).…”

Section: Introductionmentioning

confidence: 99%

Photocoagulation of Human Plasma: Acyl Serine Proteinase Photochemistry

Porter

Bruhnke

1990

Photochem & Photobiology

View full text Add to dashboard Cite

Human alpha-thrombin or bovine Factor Xa was acylated at the active site serine hydroxyl with alpha-methyl-2-hydroxy-4-diethylaminocinnamic acid. These modified serine proteinase enzymes showed no plasma coagulation biological activity in the absence of light. Photolysis of the acyl serine proteinase enzymes in plasma for 1-35 s with monochromatic 366 nm light isolated from a high pressure mercury arc results in coagulation of the plasma. For example, photolysis of 3 NIH U of the acyl human alpha-thrombin for 5 s in human plasma results in a clot in 23 s. For comparison, 1 NIH U of unmodified human alpha-thrombin gave a clot in 21 s under the conditions of the assay but without photolysis. Appropriate controls showed that the coagulation is the result of the formation of active thrombin due to photodeacylation of the enzymes. The photoinduced clotting time measured is dependent on acyl thrombin concentration and photolysis time. Thus higher concentrations of acyl thrombin and longer photolysis times give a shorter clotting time. A kinetic scheme based upon Lineweaver-Burke analysis of the clotting process is developed.

show abstract

Detection of light signals by microencapsulated cis-cinnamoyl chymotrypsin

Cited by 4 publications

References 18 publications

Encapsulation of proteins by layer‐by‐layer adsorption of polyelectrolytes onto protein aggregates: Factors regulating the protein release

Encapsulation of proteins by layer‐by‐layer adsorption of polyelectrolytes onto protein aggregates: Factors regulating the protein release

Inhibition or initiation of a radical polymerization reaction by an ultraviolet‐induced enzymatic process

Photocoagulation of Human Plasma: Acyl Serine Proteinase Photochemistry

Contact Info

Product

Resources

About