Chondroitin O-methyl ester: An unusual substrate for chondroitin AC lyase

Fikri Y. Avci; Toshihiko Toida; Robert J. Linhardt

doi:10.1016/S0008-6215(03)00348-3

Chondroitin O-methyl ester: An unusual substrate for chondroitin AC lyase

Fikri Y. Avci
, Toshihiko Toida
, Robert J. Linhardt

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Chondroitin O-methyl ester was depolymerized by chondroitin AC lyase (EC 4.2.2.5) from Flavobacterium heparinum. The major product isolated from the depolymerization reaction was found to be methyl α -L-threo-hex-4-enopyranosyluronate-(1→4)-2-acetamido-2-deoxy-α, β-D-galactopyranoside.

Original language	English
Pages (from-to)	2101-2104
Number of pages	4
Journal	Carbohydrate Research
Volume	338
Issue number	20
DOIs	https://doi.org/10.1016/S0008-6215(03)00348-3
State	Published - 26 Sep 2003
Externally published	Yes

Keywords

Chondroitin AC lyase
Chondroitin O-methyl ester
Flavobacterium heparinum

Access to Document

10.1016/S0008-6215(03)00348-3

Cite this

@article{f9d318480376477899d60233588e43d9,

title = "Chondroitin O-methyl ester: An unusual substrate for chondroitin AC lyase",

abstract = "Chondroitin O-methyl ester was depolymerized by chondroitin AC lyase (EC 4.2.2.5) from Flavobacterium heparinum. The major product isolated from the depolymerization reaction was found to be methyl α -L-threo-hex-4-enopyranosyluronate-(1→4)-2-acetamido-2-deoxy-α, β-D-galactopyranoside.",

keywords = "Chondroitin AC lyase, Chondroitin O-methyl ester, Flavobacterium heparinum",

author = "Avci, \{Fikri Y.\} and Toshihiko Toida and Linhardt, \{Robert J.\}",

year = "2003",

month = sep,

day = "26",

doi = "10.1016/S0008-6215(03)00348-3",

language = "English",

volume = "338",

pages = "2101--2104",

journal = "Carbohydrate Research",

issn = "0008-6215",

publisher = "Elsevier Ltd.",

number = "20",

}

TY - JOUR

T1 - Chondroitin O-methyl ester

T2 - An unusual substrate for chondroitin AC lyase

AU - Avci, Fikri Y.

AU - Toida, Toshihiko

AU - Linhardt, Robert J.

PY - 2003/9/26

Y1 - 2003/9/26

N2 - Chondroitin O-methyl ester was depolymerized by chondroitin AC lyase (EC 4.2.2.5) from Flavobacterium heparinum. The major product isolated from the depolymerization reaction was found to be methyl α -L-threo-hex-4-enopyranosyluronate-(1→4)-2-acetamido-2-deoxy-α, β-D-galactopyranoside.

AB - Chondroitin O-methyl ester was depolymerized by chondroitin AC lyase (EC 4.2.2.5) from Flavobacterium heparinum. The major product isolated from the depolymerization reaction was found to be methyl α -L-threo-hex-4-enopyranosyluronate-(1→4)-2-acetamido-2-deoxy-α, β-D-galactopyranoside.

KW - Chondroitin AC lyase

KW - Chondroitin O-methyl ester

KW - Flavobacterium heparinum

UR - https://www.scopus.com/pages/publications/0141671620

U2 - 10.1016/S0008-6215(03)00348-3

DO - 10.1016/S0008-6215(03)00348-3

M3 - Article

C2 - 14505877

AN - SCOPUS:0141671620

SN - 0008-6215

VL - 338

SP - 2101

EP - 2104

JO - Carbohydrate Research

JF - Carbohydrate Research

IS - 20

ER -

Chondroitin O-methyl ester: An unusual substrate for chondroitin AC lyase

Abstract

Keywords

Access to Document

Fingerprint

Cite this