Effect of ultraviolet irradiation on susceptibility of serum albumins to trypsin

A - Papers appearing in refereed journals

Kleczkowski, A. 1964. Effect of ultraviolet irradiation on susceptibility of serum albumins to trypsin. Photochemistry and Photobiology. 3 (2), pp. 115-120. https://doi.org/10.1111/j.1751-1097.1964.tb07860.x

AuthorsKleczkowski, A.
Abstract

Ultraviolet irradiation converts bovine serum albumin (BSA) and rabbit serum albumin (RS A) into forms much more rapidly hydrolysed by trypsin than the original proteins. The radiation energy (at 2537Å) required to be absorbed by each mg of a protein to convert half of it into a form susceptible to trypsin (E50%) is about 0.32 J for BSA and 0.62 J for RSA. The average E50% for inactivation of enzymes and antibodies is 0.7 J so the two processes may depend on similar alterations in irradiated protein molecules. The alteration can be considered as denaturation, with protein molecules becoming at least partially unfolded and making the sites susceptible to the attack by trypsin more easily accessible to the enzyme.

Year of Publication1964
JournalPhotochemistry and Photobiology
Journal citation3 (2), pp. 115-120
Digital Object Identifier (DOI)https://doi.org/10.1111/j.1751-1097.1964.tb07860.x
Open accessPublished as non-open access
Output statusPublished
Publication dates
Print01 Jun 1964
ISSN1751-1097
PublisherWiley

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