Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica.

Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica. Research Abstract Details 

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Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica. Abstract Text:

K Watanabe,Y Suemasu,G Funatsu,

Luffin-a, a ribosome-inactivating protein from the seeds of sponge gourd (Luffa cylindrica), was modified with 2,4,6-trinitrobenzenesulfonic acid (TNBS) at pH 8.0 and 20 degrees C. The inhibitory activity of the modified luffin-a on protein synthesis using rabbit reticulocyte lysate was lost rapidly at a rate compatible with that of the modification of a single highly reactive amino group in the initial stage of the reaction. By cation-exchange FPLC of the products of 5-min modification, TNP-luffin-a containing one modified amino group was obtained and shown to have only 6.7% of the activity of native luffin-a without any gross conformational change. The amino acid composition and sequence of the TNP-peptide, isolated by reverse-phase HPLC of the tryptic digest of the TNP-luffin-a, unambiguously demonstrate the trinitrophenylation of lysine residue at position 231. From these results, it was concluded that Lys231 of luffin-a is highly reactive to TNBS and is located at or near the active site of luffin-a.

Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica. Publishing Authors By Initials

K Watanabe,Y Suemasu,G Funatsu,

For similar organic chemicals: hydrocarbons: hydrocarbons, cyclic: hydrocarbons, aromatic: benzene derivatives: nitrobenzenes: trinitrobenzenes: trinitrobenzenesulfonic acid research abstracts see: organic chemicals: hydrocarbons: hydrocarbons, cyclic: hydrocarbons, aromatic: benzene derivatives: nitrobenzenes: trinitrobenzenes: trinitrobenzenesulfonic acid research

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Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 106

Page Numbers: 977-81

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1989

Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica. Keywords Mesh Terms:

KEYWORDS: Trinitrobenzenesulfonic Acid

MESH TERMS: metabolism

Chemical & Substance for Abstract: Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica. Information

Substance Name: Lysine

Registry Number: 56-87-1

Grant and Affiliation Information for Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica.

AFFILIATION: Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka.

Country: JAPAN

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MEDLINETA: J Biochem

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