Further studies on the primer formation for glycogen biosynthesis in rat heart.

Using selected incubation conditions we have identified intermediate steps, between the first glucose transferred to protein and the appropriate substrate for glycogen synthase. Mn2+ stimulates the addition of the first, and probably, the second glucose molecule to the acceptor protein but inhibits...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Tolmasky, D.S., Salmoral, E.M., Blumenfeld, M.L., Krisman, C.R.
Formato: JOUR
Materias:
rat
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_01455680_v39_n3_p301_Tolmasky
Aporte de:
id todo:paper_01455680_v39_n3_p301_Tolmasky
record_format dspace
spelling todo:paper_01455680_v39_n3_p301_Tolmasky2023-10-03T14:59:54Z Further studies on the primer formation for glycogen biosynthesis in rat heart. Tolmasky, D.S. Salmoral, E.M. Blumenfeld, M.L. Krisman, C.R. 1,4 glucan 1,4-glucan glucan glucose glucosyltransferase glycogen glycogen synthase glycogenin glycoprotein manganese animal article biosynthesis heart muscle metabolism rat Animals Glucans Glucose Glucosyltransferases Glycogen Glycogen Synthase Glycoproteins Manganese Myocardium Rats Using selected incubation conditions we have identified intermediate steps, between the first glucose transferred to protein and the appropriate substrate for glycogen synthase. Mn2+ stimulates the addition of the first, and probably, the second glucose molecule to the acceptor protein but inhibits further elongation. In the presence of Mn2+ only one radioglucosylated protein band of M(r) 42 kDa was evident. In the absence of Mn2+, two bands of 60.7 and 64.6 kDa were obtained indicating elongation of the glucan chains. After Glc6P addition a family of glucosylated proteins with higher M(r) was obtained, as reported previously. Mn2+ inhibition of the second step, is reversed by PMSF+Glc6P addition. Under these conditions a family of radioglucosylated protein bands with M(r) far in excess of 42 kDa, similar to that obtained without Mn2+, was obtained. Therefore, two different transglucosylating activities were necessary, at least, to prepare the appropriate substrate for glycogen synthase. Based on these observations the model we proposed earlier for glycogen biogenesis is modified. The original "Glycogen Initiator" implies at present two enzymatic activities, Glycogen Initiator 1 (activated by Mn2+) and Glycogen Initiator 2 (inhibited by Mn2+). Fil:Tolmasky, D.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Blumenfeld, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Krisman, C.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01455680_v39_n3_p301_Tolmasky
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 1,4 glucan
1,4-glucan
glucan
glucose
glucosyltransferase
glycogen
glycogen synthase
glycogenin
glycoprotein
manganese
animal
article
biosynthesis
heart muscle
metabolism
rat
Animals
Glucans
Glucose
Glucosyltransferases
Glycogen
Glycogen Synthase
Glycoproteins
Manganese
Myocardium
Rats
spellingShingle 1,4 glucan
1,4-glucan
glucan
glucose
glucosyltransferase
glycogen
glycogen synthase
glycogenin
glycoprotein
manganese
animal
article
biosynthesis
heart muscle
metabolism
rat
Animals
Glucans
Glucose
Glucosyltransferases
Glycogen
Glycogen Synthase
Glycoproteins
Manganese
Myocardium
Rats
Tolmasky, D.S.
Salmoral, E.M.
Blumenfeld, M.L.
Krisman, C.R.
Further studies on the primer formation for glycogen biosynthesis in rat heart.
topic_facet 1,4 glucan
1,4-glucan
glucan
glucose
glucosyltransferase
glycogen
glycogen synthase
glycogenin
glycoprotein
manganese
animal
article
biosynthesis
heart muscle
metabolism
rat
Animals
Glucans
Glucose
Glucosyltransferases
Glycogen
Glycogen Synthase
Glycoproteins
Manganese
Myocardium
Rats
description Using selected incubation conditions we have identified intermediate steps, between the first glucose transferred to protein and the appropriate substrate for glycogen synthase. Mn2+ stimulates the addition of the first, and probably, the second glucose molecule to the acceptor protein but inhibits further elongation. In the presence of Mn2+ only one radioglucosylated protein band of M(r) 42 kDa was evident. In the absence of Mn2+, two bands of 60.7 and 64.6 kDa were obtained indicating elongation of the glucan chains. After Glc6P addition a family of glucosylated proteins with higher M(r) was obtained, as reported previously. Mn2+ inhibition of the second step, is reversed by PMSF+Glc6P addition. Under these conditions a family of radioglucosylated protein bands with M(r) far in excess of 42 kDa, similar to that obtained without Mn2+, was obtained. Therefore, two different transglucosylating activities were necessary, at least, to prepare the appropriate substrate for glycogen synthase. Based on these observations the model we proposed earlier for glycogen biogenesis is modified. The original "Glycogen Initiator" implies at present two enzymatic activities, Glycogen Initiator 1 (activated by Mn2+) and Glycogen Initiator 2 (inhibited by Mn2+).
format JOUR
author Tolmasky, D.S.
Salmoral, E.M.
Blumenfeld, M.L.
Krisman, C.R.
author_facet Tolmasky, D.S.
Salmoral, E.M.
Blumenfeld, M.L.
Krisman, C.R.
author_sort Tolmasky, D.S.
title Further studies on the primer formation for glycogen biosynthesis in rat heart.
title_short Further studies on the primer formation for glycogen biosynthesis in rat heart.
title_full Further studies on the primer formation for glycogen biosynthesis in rat heart.
title_fullStr Further studies on the primer formation for glycogen biosynthesis in rat heart.
title_full_unstemmed Further studies on the primer formation for glycogen biosynthesis in rat heart.
title_sort further studies on the primer formation for glycogen biosynthesis in rat heart.
url http://hdl.handle.net/20.500.12110/paper_01455680_v39_n3_p301_Tolmasky
work_keys_str_mv AT tolmaskyds furtherstudiesontheprimerformationforglycogenbiosynthesisinratheart
AT salmoralem furtherstudiesontheprimerformationforglycogenbiosynthesisinratheart
AT blumenfeldml furtherstudiesontheprimerformationforglycogenbiosynthesisinratheart
AT krismancr furtherstudiesontheprimerformationforglycogenbiosynthesisinratheart
_version_ 1782027619393339392