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Lakhtin V., Lakhtin M., Aleshkin V. INTERACTION OF Lakhtin V., Lakhtin M., Aleshkin V. G.N. Gabrichevsky Research Institute for Epidemiology and Microbiology, Russia INTERACTION OF GLYCOSIDASES WITH CARBOHYDRATE-SENSITIVE REAGENTS Summary. The data on glycobiological aspects of 68 glycosidasases (interacting with carbohydrate-sensitive proteins and other reagents) from 430 sources are systemized and presented as a table. Key words: glycosidases, lectins, glycoconjugate recognition, biotechnology, microbiology, medicine. The data on at least 68 exo- and endoglycosidases from more than 430 sources are presented in the table (see below). Isolation of glycosidases using lectins The use of ConA-sorbents was especially effective for isolation of: shrimp chitinase (40 fold [f]) [905], bovine testicular lysosomal sialidase (25 f) [923], human placental lysosomal alpha- glucosidase (127 f) [960], human liver acid alpha-glucosidase (35-54 f) [707], flax linustatinase and linamarase as cyanogenic beta-glucosidases (32-44 f) [1276], human placental lysosomal alpha- glucosidase (146 f) [960], leguminous seed alpha-galactosidases (22-80 f) [972, 973, 977], human liver or placental acid beta-galactosidases (107-166 f) [960, 984, 985], feline or human liver lysosomal beta-galactosidase (45-78 f) [999, 1000, 1002, 1003], human liver acid beta-galactosidase of the patient with GM1-gangliosidosis (344 f) [1006], human placental acid beta-galactosidases (127-167 f) [1011, 924], wheat grain aleuronic alpha-mannosidase (49 f) [1034], mussel hepatopancreatic Zn2+-dependent alpha-mannosidase (71 f) [1037], human placental acid alpha- mannosidase (109 f) [960], goat kidney lysosomal alpha-mannosidase (27 f) [1056], mung bean beta- fructofuranosidase (40-90 f) [1107, 1109], pea beta-N-acetyl-D-glucosaminidases (70 f) [1031], human placental acid beta-N-acetyl-D-glucosaminidase (119 f) [960], ficus latex beta-N-acetyl-D- glucosaminidase (110 f) [1166], pea seed beta-N-acetyl-D-glucosaminidases (137-250 f) [1170], human placental acid beta-N-acetyl-D-hexoseaminidases (45-63 f) [1193, 1201], human spleen acid beta-N-acetyl-D-hexoseaminidases (40 f) [1208], human liver acid alpha-L-arabinofuranosidase (35- 54 f) [707], human lung alpha-L-iduronidase (540 f) [1242], and white mustard seed myrosinase (33 f) [1302]. The use of WGA-sorbents was especially effective in islolation of: wheat (endogenic) grain aleuronic beta-galactosidases (48 f) [991], human liver acid alpha-mannosidase (93 f) [707], fungal beta-N-acetyl-D-glucosaminidase (33 f) [968], wheat (endogenic) grain beta-N-acetyl-D- glucosaminidase (34 f) [1174], and human liver lactosylceramidase-II (75 f) [707]. LCA-sorbents were useful for isolation and multiple forms separation of: lentil alpha- galactosidase forms [979], bacteriophage hyaluronidase [1132], parasitical nematode beta-N-acetyl- D-hexososaminidase (10 f) [1182], and calf thyroid gland plasma membrane bound NAD- glycohydrolase [1295]. Other immobilized lectins were effective for the isolation of rat liver lysosomal alpha- glucosidase (RCA-sorbent, 36 fold) [617], influenza virion sialidase (CJA-I-sorbent) [918]. In many cases glycosidases were activated during lectin chromatography. Thus, slight activation (up to 10%) was observed in the cases of sorghum cyanogenic beta-glucosidase (dhurrinase) or black cherry prunasine hydrolases filtrated through ConA-sorbent [1275, 1278], human placental lysosomal alpha-glucosidase [960], chicken liver or bovine brain beta-galactosidases [995, 996], human cytosolic alpha-mannosidase filtrated through lectin sorbent [1042], monkey testicular 1 hyaluronidase [1139], or potato tuber beta-fructofuranosidase [1104]. Significant levels of glycosidase activation were registrated in the following cases: rabbit kidney neutral beta-glucosidase filtrated through lectin sorbent (18% activation) [962], human placental beta-galactosidase (50%) [985], human liver acid beta-galactosidase of the patient with GM1- gangliosidosis (few fold activation) [1006], rabbit kidney neutral beta-galactosidase filtrated through lectin sorbent (18% activation) [962], guinea pig liver acid alpha-mannosidase (42% activation) [1059], potato tuber beta-fructofuranosidase (84% activation) [1105]. Interestingly, activator(s) of glycosidases can be also activated during lectin chromatography, as it was shown for glucosylceramidase activator proteins from human spleen (up to 30%) [1148]. Thus, glycosidase activation can be influenced by elimination of glycosidase inhibitor(s) [1105], or the presence of endogenic activating factors. In a number cases, glycosidase activation was accompanied with significant levels of enzyme purification at the step of lectin chromatography [960, 985, 1005, 1106]. A lot of examples on separation of enzyme multiple forms can be found in the table. For example, mammalian lysosomal (acid) glycosidase forms with affinity to lectins can be simply separated from cytosolic (neutral) glycosidase forms without affinity to the same lectins [707, 958, 962, 1192, 1216]. Fungal purified glycosidase forms having similar sugar composition can be further separated on lectin sorbent using elution with sugar gradient [876]. A set of lectins allows to reveal or separate glycosidase forms, as it was demonstrated for human liver acid beta-galactosidase [1008], radish or castor bean beta-fructofuranosidases [1098, 1103], sweet wormwood or rat liver beta-N- acetyl-D-glucosaminidases [952, 1128], human intestinal sucrase-isomaltase [892]. Interestingly, mutual conversion of isoenzyme forms can take place [828, 1008]. Sometimes, glycosidases reveal strong binding to lectin sorbents. For example, immobilization of fungal beta-glucosidase on ConA-Macrosorb has taken place even in the presence of 0,5 M lectin- specific sugar and 10% ethanol [949]. In another cases the presence of ethylene glycol or borate together with sugar was needed for successful elution of glycosidases bound to lectin sorbents [1190, 1118]. Retaining of glycosidase activity of enzyme bound to lectin allows using lectin matrixes as affinity carriers for preparing biocatalysts (see Chapter 1). Sometimes, low affinity interaction between glycosidases and lectin sorbents result in enzyme or enzyme form retardation in eluates without use of sugar for elution [952, 968, 1098]. Interestingly, a number of glycopeptides and glycans from glycoproteins can be retarded during lectin chromatography, depending on glycan structure and lectin type (see Chapter 1). Coupled/ sequential column technique was applied for purification of the following glycosidases: bacterial cell wall zymogenic form of lysozyme (combination of immobilized hemoglobin and ConA, 62 f) [914], trichinella larval beta-N-acetyl-D-hexoseaminidases (filtration through DEAEC followed by affinity chromatography on LCA-sorbent) [1182], human liver lysosomal alpha-L-iduronidase (ConA and Blue agarose, 380 f) [1241]. Few cases include the use of lectin sorbents for immobilization of ligands interacting with glycosidases (for "sandwich" chromatography of glycosidases) [1069, 1070, 1238, 1253]. It shoud be noted that the use of lectins (RCA-I and others) in study of pathological forms of glycosidases may be of diagnostical significanca. Examples of glycosidases from human tissues and cell lines from patients with liver disorders, I-cell disease, mucolipidosis-II, GM1 gangliosidosis, leukaemic diseases can be found in the general table. Glycosidases can interact with endogenic lectins [1019, 1174, 1196, 1219]. As a result of glycosidase-lectin complexes, modulation of glycosidase activity can be revealed (see Chapter 1). Carbohydrate moiety of glycosidases As for other enzyme classes and esterases described above, carbohydrate moiety of glycosidases are characterized as wide varying one: from very low contents (<1% w/w) in cases of bacterial beta- 2 amylase [812], fungal beta-glucosidase [946], or rat liver mannosidase-I from Golgi apparatus [1271] up to 45-80% in the cases of Aspergillus cellulaes and beta-glucosidase [861, 938], yeast glucoamylase [847], beta-fructofuranosidase [1065] and exo-beta-1,3-D-glucanase [1231], or castor bean beta-fructofuranosidase [1102]. Interestingly, too low sugar content does not allow to interact with lectin properly. In such cases special conditions are needed. Thus, Man9GlcNAc-splitting alpha-mannosidase must be incubated with ConA-sorbent for 16 hours to increase its binding ability from 0 up to 70% [1271]. Specific interaction in this case was supported by experiment with EndoH-treated enzyme which lost ability for further interaction with lectin. On the other hand, polysaccharide-associated enzyme with relatively high content of sugars can not interact with the same lectin. Thus, Candida exo-beta-D-glucanase treated with beta-glucosidase reveals ability to be precipitated with ConA [1231]. However, native enzyme (68% sugars, mainly glucose and mannose) does not bind to ConA-sorbent nor be precipitated with non-immobilized lectin [1231]. In some cases carbohydrate composition of glycosidase sanples was characterized by the presence of L-rhamnose [813, 910], L-arabinose [971], or both sugars [976]. However, many microbial glycosidases include sugar residues which are typical for glycans linked to proteins [280, 692, 866, 898, 987, 1161]. That is why the use of carbohydrate-binding proteins in study of glycosidases would be of special interest for further glycan structure analysis or separation of glycosidase multiple forms. A set of lectins with specificities needed can be selected from the table. Carbohydrate moiety of
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