Photochemistry of Proteins. X. The Influence of Reagents and Conditions on the Quantum Yield for the Inactivation-denaturation of Chymotrypsin

McLaren, A. D.; Finkelstein, Paul

doi:10.1021/ja01168a016

Cited by 29 publications

(5 citation statements)

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“…(2) We have also found a similar 'damaged' class of molecules in autolyzed trypsin and in trypsin treated with gamma radiati~n. (~,l~) Analogous 'damaged' classes of proteins as detected by an increased temperature sensitivity have been reported for photodynamically treated myosin and pepsin@) and for u.v.-treated chymotrypsin (8)…”

Section: Discussionmentioning

confidence: 68%

The Photoinactivation of Trypsin as Sensitized by Methylene Blue and Eosin Y*

Ghiron

Spikes

1965

Photochem & Photobiology

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Abstract— The kinetics of the photoinactivation of trypsin as sensitized by methylene blue and by eosin Y were investigated. The time‐course of inactivation was first‐order. The rates of inactivation were essentially identical as measured by three methods: the casein assay, the benzoyl‐L‐arginine ethyl ester assay, and the hemoglobin (in 5 M urea) assay. This is in sharp contrast to the results of earlier studies with flavins as photosensitizers, where the rate of inactivation was found to be much greater when measured by the hemoglobin assay than when measured by the other two assays. These differences are interpreted as indicating the production of a urea‐sensitive ‘damaged class’ of trypsin molecules during photodynamic inactivation with flavins as sensitizers, but not with methylene blue and eosin Y. The results presented indicate that the mechanism of the photodynamic inactivation of enzymes might be different with different photosensitizing dyes.

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Section: Discussionmentioning

confidence: 68%

The Photoinactivation of Trypsin as Sensitized by Methylene Blue and Eosin Y*

Ghiron

Spikes

1965

Photochem & Photobiology

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“…The earliest studies on the association properties of chymotrypsin derivatives involved the use of relatively nonspecific or poorly characterized modifications. McLaren and Finkelstein (1950) observed greatly decreased sedimentation coefficients and activity upon 235-mp irradiation of chymotrypsin.…”

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confidence: 97%

Low pH dimerization behavior of active-site derivatives of bovine α-chymotrypsin

Ta¹,

Dc²

1973

Biochemistry

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“…- 49-temperature has been shown to affect the apparent quantum yield for the ultraviolet radiation inactivation of chymotrypsin (106). In the present case, the temperature during the assay was varied over the range.5-390 C without producing any app arent differences in the rate of the photodynamic inactivation of trypsin (Fig.…”

Section: -1mentioning

confidence: 77%

Quantum Yield Studies of the Photodynamic Inactivation of Trypsin

Glad¹,

Spikes²

1964

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Photochemistry of Proteins. X. The Influence of Reagents and Conditions on the Quantum Yield for the Inactivation-denaturation of Chymotrypsin

Cited by 29 publications

References 1 publication

The Photoinactivation of Trypsin as Sensitized by Methylene Blue and Eosin Y*

The Photoinactivation of Trypsin as Sensitized by Methylene Blue and Eosin Y*

Low pH dimerization behavior of active-site derivatives of bovine α-chymotrypsin

Quantum Yield Studies of the Photodynamic Inactivation of Trypsin

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