Active centres

1989 ◽

Vol 54 (11) ◽

pp. 2933-2950

Author(s):

Emerich Erdös ◽

Petr Voňka ◽

Josef Stejskal ◽

Přemysl Klíma

Keyword(s):

Experimental Data ◽

Gallium Arsenide ◽

Kinetic Study ◽

Gas Phase ◽

Growth Model ◽

Epitaxial Layers ◽

Inhomogeneous Model ◽

Homogeneous Models ◽

Active Centres

This paper represents a continuation and ending of the kinetic study of the gallium arsenide formation, where a so-called inhomogeneous model is proposed and quantitatively formulated in five variants, in which two kinds of active centres appear. This model is compared both with the experimental data and with the previous sequence of homogeneous models.

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Active centres over hzsm5 zeolites for paraffin cracking

Applied Catalysis ◽

10.1016/s0166-9834(00)83325-4 ◽

1984 ◽

Vol 13 (1) ◽

pp. 27-38 ◽

Cited By ~ 33

Author(s):

R.B. Borade ◽

S.G. Hegde ◽

S.B. Kulkarni ◽

P. Ratnasamy

Keyword(s):

Active Centres

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Debranching enzyme from rabbit skeletal muscle; Evidence for the location of two active centres on a single polypeptide chain

FEBS Letters ◽

10.1016/0014-5793(75)80254-7 ◽

1975 ◽

Vol 58 (1-2) ◽

pp. 181-185 ◽

Cited By ~ 50

Author(s):

Edna J. Bates ◽

Gillian M. Heaton ◽

Carol Taylor ◽

John C. Kernohan ◽

Philip Cohen

Keyword(s):

Skeletal Muscle ◽

Polypeptide Chain ◽

Rabbit Skeletal Muscle ◽

Debranching Enzyme ◽

Single Polypeptide Chain ◽

Single Polypeptide ◽

Active Centres

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Evidence that the active centre of chymopapain A is different from the active centres of some other cysteine proteinases and that the Brønsted coefficient (βnuc.) for the reactions of thiolate anions with 2,2′-dipyridyl disulphide may be decreased by reagent protonation

Biochemical Journal ◽

10.1042/bj1890189 ◽

1980 ◽

Vol 189 (1) ◽

pp. 189-192 ◽

Cited By ~ 3

Author(s):

K Brocklehurst ◽

B S Baines ◽

M S Mushiri

Keyword(s):

Carica Papaya ◽

Cysteine Proteinases ◽

Active Centre ◽

Pka Values ◽

Nitrobenzoic Acid ◽

Specific Reactivity ◽

Ph Range ◽

Thiolate Anions ◽

Active Centres

The active centres of chymopapains A and B (jointly designated EC 3.4.22.6) and papaya (Carica papaya L.) peptidase A were investigated by using 2,2′-dipyridyl disulphide and 5,5′-dithiobis-(2-nitrobenzoic acid) as thiol-specific reactivity probes. Whereas the first active-centre pKa values for chymopapain B and papaya peptidase A are less than 5, is as the case for papain (EC 3.4.22.2) and ficin (EC 3.4.22.3), that for chymopapain A is about 6.8. The reason why the reactions of thiols of pKa approx. 6.5 with 2.2′-dipyridyl disulphide are essentially pH-independent in the pH range around the thiol pKa is delineated. The value of the Brønsted coefficient (beta nuc.) for the reactions of thiolate ions with the 2,2′-dipyridyl disulphide monocation appears to be smaller than its value for the corresponding reactions with the neutral disulphide.

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