Conformational changes of papain induced on interaction with thiol proteinase inhibitors from newborn rat epidermis.

Conformational changes of papain induced on interaction with thiol proteinase inhibitors from newborn rat epidermis. Research Abstract Details 

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Conformational changes of papain induced on interaction with thiol proteinase inhibitors from newborn rat epidermis. Abstract Text:

A Takeda,S Kobayashi,H Kaji,Y Aoki,T Samejima,

The conformational changes of the papain molecular on interaction with two thiol proteinase inhibitors (TPI(1) and TPI(2] from newborn rat epidermis were studied by measuring circular dichroism (CD), the difference absorption spectrum, and the fluorescence spectrum due to tryptophan residues in papain. The far-ultraviolet CD band of papain between 210 and 230 nm was distinctly reduced on interaction with both inhibitors. Also, the near-ultraviolet CD spectrum of TPI(1)-bound papain changed between 285 and 320 nm as well as that of the TPI(2)-bound enzyme. The difference absorption spectrum for TPI(1)-bound papain exhibited two distinct peaks at 276.5 and 282 nm, indicating perturbation of aromatic amino acid residues. The fluorescence intensity of papain was significantly decreased on interaction with both inhibitors, which showed pH-dependency on an ionizable group, with pK values of 8.5 and 7.9 for TPI(1) and TPI(2), respectively. The complex formation of papain with both inhibitors caused a reduction of the susceptibility of a tryptophan residue, probably tryptophan-177, to chemical modification with N-bromosuccinimide. These results suggest that the active site involving histidine-159 in the papain molecule was much influenced by the alteration of the microenvironment of tryptophan-177 as a part of the interaction site for these two thiol proteinase inhibitors.

Conformational changes of papain induced on interaction with thiol proteinase inhibitors from newborn rat epidermis. Publishing Authors By Initials

A Takeda,S Kobayashi,H Kaji,Y Aoki,T Samejima,

For similar amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tryptophan research abstracts see: amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tryptophan research

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Conformational changes of papain induced on interaction with thiol proteinase inhibitors from newborn rat epidermis. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 99

Page Numbers: 785-91

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Mar

YEAR: 1986

Conformational changes of papain induced on interaction with thiol proteinase inhibitors from newborn rat epidermis. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Conformational changes of papain induced on interaction with thiol proteinase inhibitors from newborn rat epidermis. Keywords Mesh Terms:

KEYWORDS: Tryptophan

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Conformational changes of papain induced on interaction with thiol proteinase inhibitors from newborn rat epidermis. Information

Substance Name: Papain

Registry Number: EC 3.4.22.2

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Country: JAPAN

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MEDLINETA: J Biochem

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