Abstract:
:The effect of a protein matrix on the processing of glycoprotein glycans by Golgi enzymes from plant seedlings has been determined with an artificial glycoprotein system, comparing the processing rates of glycan-(biotinyl)Asn (or glycan-(biotinamidohexanoyl)Asn) substrates either free or bound to avidin. An analysis of the pooled glycoproteins from the seedlings suggested that the most common glycan structure is a complex one (GlcNAc-Man3GlycNAc2-protein), and consistent with this processing end-product, mannosidases I and II and GlcNAc transferases I and II were all found to be present in the seedling Golgi membrane preparations. The effect of the avidin matrix either in a proximal (biotinyl substrates) or distal (N-(biotinamido)hexonoyl substrates) association with the appropriate glycan substrate for these four enzymes was assessed from the direct comparison of the apparent first-order rate constants for the free and avidin-bound substrate-product conversions. All four plant enzymes were inhibited by the association of the glycan substrates with avidin, but the inhibition was much less pronounced than that observed with the corresponding enzymes from rat liver and hen oviduct. The rate effect shows a progression from 3- to 10-fold rate decreases in the proximal complexes and 2- to 3-fold in the distal complexes in going from the first (mannosidase I) to the fourth (GlcNAc transferase II) enzyme; with the mammalian and avian enzymes the largest effects were for the first ones and much larger absolute rate effects were observed. The results suggest that the nature of the processing enzymes in terms of this response to the avidin glycan substrates may differ in different organisms.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Lu Y,Wold Fdoi
10.1016/0003-9861(91)90020-jsubject
Has Abstractpub_date
1991-04-01 00:00:00pages
147-52issue
1eissn
0003-9861issn
1096-0384pii
0003-9861(91)90020-Jjournal_volume
286pub_type
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更新日期:1995-01-10 00:00:00
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pub_type: 杂志文章
doi:10.1006/abbi.1994.1138
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1993-03-01 00:00:00
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pub_type: 杂志文章
doi:10.1006/abbi.1996.9784
更新日期:1997-01-15 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
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更新日期:1999-03-15 00:00:00
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pub_type: 杂志文章,评审
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更新日期:2005-01-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1016/0003-9861(84)90393-x
更新日期:1984-06-01 00:00:00
abstract::Carbohydrate Binding Modules (CBMs) targeting cellulose, xylan and mannan have been reported, however, a CBM targeting rhamnogalacturonan I (RG I) has never been identified. We had studied earlier a rhamnogalacturonan lyase (CtRGL) from Clostridium thermocellum that was associated with a family 35 CBM, Rgl-CBM35. In t...
journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:2018-09-15 00:00:00
abstract::Protein tyrosine kinase Yes is a cellular homolog of v-Yes, the oncogenic protein product of avian sarcoma virus Y73. Yes is a member of the Src family and its activation has been associated with several types of human cancer. Human Yes has not been previously characterized enzymatically. To carry out biochemical char...
journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.1997.0236
更新日期:1997-09-01 00:00:00