Boron and calcium, essential inorganic constituents of pectic polysaccharides in higher plant cell walls

1998 ◽  
Vol 111 (1) ◽  
pp. 179-190 ◽  
Author(s):  
Toru Matoh ◽  
Masaru Kobayashi
1999 ◽  
Vol 119 (1) ◽  
pp. 199-204 ◽  
Author(s):  
Masaru Kobayashi ◽  
Hironobu Nakagawa ◽  
Tomoyuki Asaka ◽  
Toru Matoh

PROTOPLASMA ◽  
1988 ◽  
Vol 143 (2-3) ◽  
pp. 165-169 ◽  
Author(s):  
G. Nagahashi ◽  
Linda Garzarella

1969 ◽  
Vol 115 (3) ◽  
pp. 431-439 ◽  
Author(s):  
D. A. Rees ◽  
N. J. Wight

Methylation analysis was used to characterize the pectic polysaccharides from mustard cotyledons, a tissue with potential for rapid biological change involving the walls. The methylated sugars were identified by g.l.c. and paper chromatography after conversion of uronic acid derivatives into [3H]hexoses, and confirmed by the formation of crystalline derivatives of most of the main products, which were: 2,3-di-O-methyl-d-[6−3H]galactose, 2-O-methyl-d-[6−3H]galactose, 3,4-di-O-methylrhamnose, 3-O-methylrhamnose, 2,3,5-tri-O-methyl-l-arabinose, 2,3-di-O-methyl-l-arabinose, 2-O-methyl-l-arabinose, 2,3,4-tri-O-methyl-d-xylose and 2,3,4,6-tetra-O-methyl-d-galactose in the molar proportions 1·00:1·14:0·54:0·74:2·86:2·50:2·24:1·88:0·32. The structural units present are similar to those in wellknown polysaccharides from mature tissues, but their proportions are strikingly different. Uninterrupted and unbranched galacturonan segments can therefore contribute little cohesion to these walls, and it is suggested that this correlates with a function of the wall matrix to hydrate and permit readjustment, during germination, of structural elements or wall surfaces or both.


1996 ◽  
Vol 110 (4) ◽  
pp. 1063-1068 ◽  
Author(s):  
G. H. Henriksen ◽  
A. R. Taylor ◽  
C. Brownlee ◽  
S. M. Assmann

2002 ◽  
Vol 68 (4) ◽  
pp. 1610-1615 ◽  
Author(s):  
Koichiro Murashima ◽  
Akihiko Kosugi ◽  
Roy H. Doi

ABSTRACT Clostridium cellulovorans produces a cellulase enzyme complex (cellulosome). In this study, we isolated two plant cell wall-degrading cellulosomal fractions from culture supernatant of C. cellulovorans and determined their subunit compositions and enzymatic activities. One of the cellulosomal fractions showed fourfold-higher plant cell wall-degrading activity than the other. Both cellulosomal fractions contained the same nine subunits (the scaffolding protein CbpA, endoglucanases EngE and EngK, cellobiohydrolase ExgS, xylanase XynA, mannanase ManA, and three unknown proteins), although the relative amounts of the subunits differed. Since only cellobiose was released from plant cell walls by the cellulosomal fractions, cellobiohydrolases were considered to be key enzymes for plant cell wall degradation.


2008 ◽  
Vol 134 (2) ◽  
pp. 237-245 ◽  
Author(s):  
John P. Moore ◽  
Mäite Vicré-Gibouin ◽  
Jill M. Farrant ◽  
Azeddine Driouich

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