Entrapment of porous and stable concanavalin A–peroxidase complex into hybrid calcium alginate–pectin gel

2006 ◽  
Vol 81 (7) ◽  
pp. 1316-1323 ◽  
Author(s):  
Mahreen Matto ◽  
Qayyum Husain
1985 ◽  
Vol 27 (8) ◽  
pp. 1102-1107 ◽  
Author(s):  
Qayyum Husain ◽  
Jawaid Iqbal ◽  
M. Saleemuddin

Author(s):  
B. Monis ◽  
D. Lis ◽  
I. Parlanti ◽  
A. R. Eynard ◽  
M. A. Valentich ◽  
...  

We are gathering evidences which indicate ultrastructural variations and chemical heterogeneity of certain glycocalyces as well as hormone dependence of some of them. Thus, in the lumenal glycocalyx of renal collecting tubules of the guinea-pig granular and filamentous structures were seen (1, fig. 1). By isolation, chemical analysis and cellulose acetate electrophoresis in various buffers of tubular membrane material, glycopeptides and glycosaminoglycans were identified (fig. 2).Guinea-pig and rat transitional epithelium of urinary tract showed a filamentous lumenal glycocalyx demonstrable with ruthenium red (fig. 3) but which only in part stained with concanavalin A. Chemical and electrophoretic data indicated that urothelium contains glycoproteins, glycosaminoglycans and glycolipids.The glycocalyx of the fat globule membrane of milk of several species has a granular appearance as shown by cationic dyes and by concanavalin A (2, 3, fig. 4 and 5). Also, several glycoproteins were isolated and identified on polyacrilamide gel electrophoresis (fig. 6). Glycosaminoglycans and certain glycolipids such as sulfatides were chemically identified in this glycocalyx.


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