Enzymatic sulfation of triglucosyl monoalkylmonoacylglycerol in rat salivary glands

B. L. Slomiany; Y. H. Liau; E. Zdebska; V. L.N. Murty; A. Slomiany

doi:10.1016/0006-291X(83)91072-0

Enzymatic sulfation of triglucosyl monoalkylmonoacylglycerol in rat salivary glands

B. L. Slomiany, Y. H. Liau, E. Zdebska, V. L.N. Murty, A. Slomiany

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

5 Scopus citations

Abstract

A sulfotransferase activity present in the cytosol fraction of rat submandibular and parotid salivary glands catalyzes the transfer of sulfate group from 3′-phosphoadenosine5′-phosphosulfate to C-6 of the terminal glucose residue of Glcαl→6Glcαl→6Glcαl→3-1, (3)-0-alkyl-2-0-acylglycerol to form sulfated triglucosyl glyceroglucolipid. The reaction proceeds at its optimum at pH 7.8, and requires the detergent Triton X-100, F^1- and Mg²⁺. The enzyme does not catalyze the sulfation of glycosphingolipids. The apparent Km of the submandibular enzyme for triglucosyl glyceroglucolipid is 78.8μM, and that of parotid, 58.8μM. Analysis of the permethylated ³⁵S-labeled enzymatic product demonstrated that the sulfate group is located at C-6 of the terminal glucose residue.

Original language	English (US)
Pages (from-to)	817-824
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	113
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(83)91072-0
State	Published - Jun 29 1983
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/0006-291X(83)91072-0

Cite this

@article{58f126834f1b4bdcbfa857fd49c13480,

title = "Enzymatic sulfation of triglucosyl monoalkylmonoacylglycerol in rat salivary glands",

abstract = "A sulfotransferase activity present in the cytosol fraction of rat submandibular and parotid salivary glands catalyzes the transfer of sulfate group from 3′-phosphoadenosine5′-phosphosulfate to C-6 of the terminal glucose residue of Glcαl→6Glcαl→6Glcαl→3-1, (3)-0-alkyl-2-0-acylglycerol to form sulfated triglucosyl glyceroglucolipid. The reaction proceeds at its optimum at pH 7.8, and requires the detergent Triton X-100, F1- and Mg2+. The enzyme does not catalyze the sulfation of glycosphingolipids. The apparent Km of the submandibular enzyme for triglucosyl glyceroglucolipid is 78.8μM, and that of parotid, 58.8μM. Analysis of the permethylated 35S-labeled enzymatic product demonstrated that the sulfate group is located at C-6 of the terminal glucose residue.",

author = "Slomiany, {B. L.} and Liau, {Y. H.} and E. Zdebska and Murty, {V. L.N.} and A. Slomiany",

note = "Funding Information: ACKNOWLEDGEMENT - This work was supported by USPH Grant National Institute of Dental Research, NIH.",

year = "1983",

month = jun,

day = "29",

doi = "10.1016/0006-291X(83)91072-0",

language = "English (US)",

volume = "113",

pages = "817--824",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "3",

}

TY - JOUR

T1 - Enzymatic sulfation of triglucosyl monoalkylmonoacylglycerol in rat salivary glands

AU - Slomiany, B. L.

AU - Liau, Y. H.

AU - Zdebska, E.

AU - Murty, V. L.N.

AU - Slomiany, A.

N1 - Funding Information: ACKNOWLEDGEMENT - This work was supported by USPH Grant National Institute of Dental Research, NIH.

PY - 1983/6/29

Y1 - 1983/6/29

N2 - A sulfotransferase activity present in the cytosol fraction of rat submandibular and parotid salivary glands catalyzes the transfer of sulfate group from 3′-phosphoadenosine5′-phosphosulfate to C-6 of the terminal glucose residue of Glcαl→6Glcαl→6Glcαl→3-1, (3)-0-alkyl-2-0-acylglycerol to form sulfated triglucosyl glyceroglucolipid. The reaction proceeds at its optimum at pH 7.8, and requires the detergent Triton X-100, F1- and Mg2+. The enzyme does not catalyze the sulfation of glycosphingolipids. The apparent Km of the submandibular enzyme for triglucosyl glyceroglucolipid is 78.8μM, and that of parotid, 58.8μM. Analysis of the permethylated 35S-labeled enzymatic product demonstrated that the sulfate group is located at C-6 of the terminal glucose residue.

AB - A sulfotransferase activity present in the cytosol fraction of rat submandibular and parotid salivary glands catalyzes the transfer of sulfate group from 3′-phosphoadenosine5′-phosphosulfate to C-6 of the terminal glucose residue of Glcαl→6Glcαl→6Glcαl→3-1, (3)-0-alkyl-2-0-acylglycerol to form sulfated triglucosyl glyceroglucolipid. The reaction proceeds at its optimum at pH 7.8, and requires the detergent Triton X-100, F1- and Mg2+. The enzyme does not catalyze the sulfation of glycosphingolipids. The apparent Km of the submandibular enzyme for triglucosyl glyceroglucolipid is 78.8μM, and that of parotid, 58.8μM. Analysis of the permethylated 35S-labeled enzymatic product demonstrated that the sulfate group is located at C-6 of the terminal glucose residue.

UR - http://www.scopus.com/inward/record.url?scp=0020539458&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020539458&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(83)91072-0

DO - 10.1016/0006-291X(83)91072-0

M3 - Article

C2 - 6575780

AN - SCOPUS:0020539458

SN - 0006-291X

VL - 113

SP - 817

EP - 824

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Enzymatic sulfation of triglucosyl monoalkylmonoacylglycerol in rat salivary glands

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this