Molecular cloning and expression of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II)

Yeon Jeong Kim; Kyoung Sook Kim; Sang Hyun Kim; Cheorl Ho Kim; Jeong Heon Ko; In Seong Choe; Shuichi Tsuji; Young Choon Lee

doi:10.1006/bbrc.1996.1660

Molecular cloning and expression of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II)

Yeon Jeong Kim
, Kyoung Sook Kim
, Sang Hyun Kim
, Cheorl Ho Kim
, Jeong Heon Ko
, In Seong Choe
, Shuichi Tsuji
, Young Choon Lee

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

79 Scopus citations

Abstract

A cDNA of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II), which has been known to exhibit much more acceptor substrate preference for glycolipid than for O-linked oligosaccharides of glycoproteins, was isolated from the human liver cDNA library by plaque hybridization using the cDNA of mouse ST3Gal II (mST3Gal II) cloned previously as a probe. Comparative analysis of this cDNA with mST3Gal II indicates 89 and 94% homologies in the nucleotide and amino acid levels, respectively, between the two sequences in the predicted coding region. Northern analysis indicated that the expression of hST3Gal II mRNA is tissue-specific, it being prominent in skeletal muscle and heart, while that in lung and kidney is very low. This enzyme expressed in COS cells showed a similiar activity with that of mST3Gal II.

Original language	English
Pages (from-to)	324-327
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	228
Issue number	2
DOIs	https://doi.org/10.1006/bbrc.1996.1660
State	Published - 12 Nov 1996
Externally published	Yes

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title = "Molecular cloning and expression of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II)",

abstract = "A cDNA of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II), which has been known to exhibit much more acceptor substrate preference for glycolipid than for O-linked oligosaccharides of glycoproteins, was isolated from the human liver cDNA library by plaque hybridization using the cDNA of mouse ST3Gal II (mST3Gal II) cloned previously as a probe. Comparative analysis of this cDNA with mST3Gal II indicates 89 and 94\% homologies in the nucleotide and amino acid levels, respectively, between the two sequences in the predicted coding region. Northern analysis indicated that the expression of hST3Gal II mRNA is tissue-specific, it being prominent in skeletal muscle and heart, while that in lung and kidney is very low. This enzyme expressed in COS cells showed a similiar activity with that of mST3Gal II.",

author = "Kim, \{Yeon Jeong\} and Kim, \{Kyoung Sook\} and Kim, \{Sang Hyun\} and Kim, \{Cheorl Ho\} and Ko, \{Jeong Heon\} and Choe, \{In Seong\} and Shuichi Tsuji and Lee, \{Young Choon\}",

year = "1996",

month = nov,

day = "12",

doi = "10.1006/bbrc.1996.1660",

language = "English",

volume = "228",

pages = "324--327",

journal = "Biochemical and Biophysical Research Communications",

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TY - JOUR

T1 - Molecular cloning and expression of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II)

AU - Kim, Yeon Jeong

AU - Kim, Kyoung Sook

AU - Kim, Sang Hyun

AU - Kim, Cheorl Ho

AU - Ko, Jeong Heon

AU - Choe, In Seong

AU - Tsuji, Shuichi

AU - Lee, Young Choon

PY - 1996/11/12

Y1 - 1996/11/12

N2 - A cDNA of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II), which has been known to exhibit much more acceptor substrate preference for glycolipid than for O-linked oligosaccharides of glycoproteins, was isolated from the human liver cDNA library by plaque hybridization using the cDNA of mouse ST3Gal II (mST3Gal II) cloned previously as a probe. Comparative analysis of this cDNA with mST3Gal II indicates 89 and 94% homologies in the nucleotide and amino acid levels, respectively, between the two sequences in the predicted coding region. Northern analysis indicated that the expression of hST3Gal II mRNA is tissue-specific, it being prominent in skeletal muscle and heart, while that in lung and kidney is very low. This enzyme expressed in COS cells showed a similiar activity with that of mST3Gal II.

AB - A cDNA of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II), which has been known to exhibit much more acceptor substrate preference for glycolipid than for O-linked oligosaccharides of glycoproteins, was isolated from the human liver cDNA library by plaque hybridization using the cDNA of mouse ST3Gal II (mST3Gal II) cloned previously as a probe. Comparative analysis of this cDNA with mST3Gal II indicates 89 and 94% homologies in the nucleotide and amino acid levels, respectively, between the two sequences in the predicted coding region. Northern analysis indicated that the expression of hST3Gal II mRNA is tissue-specific, it being prominent in skeletal muscle and heart, while that in lung and kidney is very low. This enzyme expressed in COS cells showed a similiar activity with that of mST3Gal II.

UR - https://www.scopus.com/pages/publications/0030581667

U2 - 10.1006/bbrc.1996.1660

DO - 10.1006/bbrc.1996.1660

M3 - Article

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AN - SCOPUS:0030581667

SN - 0006-291X

VL - 228

SP - 324

EP - 327

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Molecular cloning and expression of human Galβ1,3GalNAc α2,3-sialyltransferase (hST3Gal II)

Abstract

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