A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.

An improved method for the structural profiling of keratan sulfates: analysis of keratan sulfates from brain and ovarian tumors. (1/982)

A previously developed method for the structural fingerprinting of keratan sulfates (Brown et al., Glycobiology, 5, 311-317, 1995) has been adapted for use with oligosaccharides fluorescently labeled with 2-aminobenzoic acid following keratanase II digestion. The oligosaccharides are separated by high-pH anion-exchange chromatography on a Dionex AS4A-SC column. This methodology permits quantitative analysis of labeled oligosaccharides which can be detected at the sub-nanogram ( approximately 100 fmol) level. Satisfactory calibration of this method can be achieved using commercial keratan sulfate standards. Keratan sulfates from porcine brain phosphocan and human ovarian tumors have been examined using this methodology, and their structural features are discussed.  (+info)

Effect of fasting on temporal variation in the nephrotoxicity of amphotericin B in rats. (2/982)

Evidence for temporal variation in the nephrotoxicity of amphotericin B was recently reported in experimental animals. The role of food in these variations was determined by studying the effect of a short fasting period on the temporal variation in the renal toxicity of amphotericin B. Twenty-eight normally fed and 28 fasted female Sprague-Dawley rats were used. Food was available ad libitum to the fed rats, while the fasted animals were fasted 12 h before and 24 h after amphotericin B injection to minimize stress for the animals. Water was available ad libitum to both groups of rats, which were maintained on a 14-h light, 10-h dark regimen (light on at 0600 h). Renal toxicity was determined by comparing the levels of excretion of renal enzyme and the serum creatinine and blood urea nitrogen (BUN) levels at the time of the maximal (0700 h) or the minimal (1900 h) nephrotoxicity after the intraperitoneal administration of a single dose of dextrose (5%; control group) or amphotericin B (50 mg/kg of body weight; treated group) to the rats. The nephrotoxicities obtained after amphotericin B administration at both times of day were compared to the nephrotoxicities observed for time-matched controls. In fed animals, the 24-h urinary excretion of N-acetyl-beta-D-glucosaminidase and beta-galactosidase was significantly higher when amphotericin B was injected at 0700 and 1900 h. The excretion of these two enzymes was reduced significantly (P < 0.05) in fasting rats, and this effect was larger at 0700 h (P < 0.05) than at 1900 h. The serum creatinine level was also significantly higher (P < 0.05) in fed animals treated at 0700 h than in fed animals treated at 1900 h. Fasting reduced significantly (P < 0.05) the increase in the serum creatinine level, and this effect was larger in the animals treated at 0700 h. Similar data were obtained for BUN levels. Amphotericin B accumulation was significantly higher (P < 0.05) in the renal cortexes of fed rats than in those of fasted animals, but there was no difference according to the time of injection. These results demonstrated that fasting reduces the nephrotoxicity of amphotericin B and that food availability is of crucial importance in the temporal variation in the renal toxicity of amphotericin B in rats.  (+info)

Endometrial lysosomal enzyme activity in normal cycling endometrium. (3/982)

The objective of this study was to evaluate the possible role of four lysosomal enzymes in endometrial function and remodelling during the normal menstrual cycle by fluorimetric measurement (acid phosphatase, N-acetyl-beta-D-glucosaminidase, alpha-L-fucosidase and alpha-D-mannosidase). A prospective study was conducted of 45 endometrial biopsies obtained from women with normal menstrual cycles. Activity of all four enzymes was identified in human endometrium. Activity of acid phosphatase and N-acetyl-beta-D-glucosaminidase was relatively high, whilst that of alpha-L-fucosidase and alpha-D-mannosidase was low. There was no significant change in the activity of any of the four enzymes from the proliferative to the secretory phase of the cycle. This study suggests that the activity of these enzymes remains constant throughout a major portion of the normal cycle.  (+info)

Immediate and early renal function after living donor transplantation. (4/982)

BACKGROUND: In order to assess the immediate renal function after living donor transplantation, renal function was compared in eight renal allograft recipients and their living related kidney donors during the first 24 h after transplantation. METHODS: Substantial and comparable intraoperative volume loading with Ringer's acetate and mannitol was performed together with the administration of frusemide. Glomerular filtration rate (GFR) and effective renal plasma flow (ERPF) were estimated by the clearances of inulin and p-aminohippurane, respectively. Tubular reabsorptive function and injury were estimated from the clearance of lithium, the fractional excretion of sodium and the urinary excretion of N-acetyl-beta-glucosaminidase. RESULTS: One hour after completion of surgery, GFR (54 +/- 7 ml/min) and ERPF (294 +/- 35 ml/min) were only 30% lower in the grafts than in the remaining donor kidneys, increasing to similar levels within 3 h. Only minor tubular dysfunction and injury were revealed in the grafted kidneys, and these tended to normalize within 24 h. CONCLUSIONS: By the present transplantation procedure comprising short ischaemia time and substantial volume expansion combined with mannitol and frusemide administration, kidneys from living donors regain nearly normal function within a few hours after transplantation.  (+info)

Active site characterization of the exo-N-acetyl-beta-D- glucosaminidase from thermotolerant Bacillus sp. NCIM 5120: involvement of tryptophan, histidine and carboxylate residues in catalytic activity. (5/982)

The exo-N-acetyl-beta-d-glucosaminidase (EC 3.2.1.30) from thermotolerant Bacillus sp. NCIM 5120 is a homotetramer with a molecular mass of 240000 kDa. Chemical modification studies on the purified exo-N-acetyl-beta-d-glucosaminidase revealed the involvement of a single tryptophan, histidine and carboxylate, per monomer, in the catalytic activity of the enzyme. Spectral analysis and maintenance of total enzyme activities indicated that N-acetylglucosamine (competitive inhibitor) and p-nitrophenyl-N-acetyl-beta-d-glucosaminide (substrate) prevented the modification of a single essential tryptophan, histidine and carboxylate residue. Kinetic parameters of partially inactivated enzyme (by NBS/HNBB) showed the involvement of tryptophan in substrate binding while that of histidine (by photooxidation/DEPC) and carboxylate (by EDAC/WRK) in catalysis. The Bacillus sp. NCIM 5120 exo-N-acetyl-beta-d-glucosaminidase deviates from the reported N-acetyl-beta-d-glucosaminidases and beta-hexosaminidases that utilize anchimeric assistance in their hydrolytic mechanism.  (+info)

Sanfilippo type B syndrome (mucopolysaccharidosis III B): allelic heterogeneity corresponds to the wide spectrum of clinical phenotypes. (6/982)

Sanfilippo B syndrome (mucopolysaccharidosis IIIB, MPS IIIB) is caused by a deficiency of alpha-N-acetylglucosaminidase, a lysosomal enzyme involved in the degradation of heparan sulphate. Accumulation of the substrate in lysosomes leads to degeneration of the central nervous system with progressive dementia often combined with hyperactivity and aggressive behaviour. Age of onset and rate of progression vary considerably, whilst diagnosis is often delayed due to the absence of the pronounced skeletal changes observed in other mucopolysaccharidoses. Cloning of the gene and cDNA encoding alpha-N-acetylglucosaminidase enabled a study of the molecular basis of this syndrome. We were able to identify 31 mutations, 25 of them novel, and two polymorphisms in the 40 patients mostly of Australasian and Dutch origin included in this study. The observed allellic heterogeneity reflects the wide spectrum of clinical phenotypes reported for MPS IIIB patients. The majority of changes are missense mutations; also four nonsense and nine frameshift mutations caused by insertions or deletions were identified. Only five mutations were found in more than one patient and the observed frequencies are well below those observed for the common mutations in MPS IIIA. R643C and R297X each account for around 20% of MPS IIIB alleles in the Dutch patient group, whilst R297X, P521L, R565W and R626X each have a frequency of about 6% in Australasian patients. R643C seems to be a Dutch MPS IIIB allele and clearly confers the attenuated phenotype. One region of the gene shows a higher concentration of mutations, probably reflecting the instability of this area which contains a direct repeat. Several arginine residues seem to be 'hot-spots' for mutations, being affected by two or three individual base pair exchanges.  (+info)

Effect of age on urinary excretion of N-acetyl-beta-D-glucosaminidase. (7/982)

To examine the relationship between the concentrations of urinary NAG and age, we measured ratios of urinary N-acetyl-beta-D-glucosaminidase (NAG) to urinary creatinine (NAG index) in 137 healthy subjects, aged from 19 to 88 years. The study is also designed to evaluate the relationship between urinary NAG and blood pressure. The subjects were divided into 7 subgroups, according to their age (< 30, 30-39, 40-49, 50-59, 60-69, 70-79, 80 or more years). There was a positive correlation between NAG index and age (r = 0.36; P < 0.001). The regression equation relating NAG index (y) to age (x) was y = 0.065x + 0.97. The mean NAG indexes for the 7 subgroups divided by age were significantly different (P < 0.01). There was a positive correlation between NAG index and systolic blood pressure (r = 0.18; P < 0.05), but was not between diastolic blood pressure and NAG index. In multiple regression analysis, age and BUN significantly correlated with NAG index (r = 0.32; P < 0.01, r = 3.3; P = 0.07, respectively), although there was no correlation between systolic blood pressure and NAG index. This cross-sectional study showed a clear elevation in NAG index with age. The rate of elevation was 0.65 per decade. Urinary excretion of NAG may be unrelated to blood pressure.  (+info)

A quantitative study of pinocytosis and lysosome function in experimentally induced lysosomal storage. (8/982)

The highly pinocytic epithelial cells of the visceral yolk sac from 17.5-day rat conceptuses were used as a model in which to induce engorgement of the vacuolar system by direct accumulation of substances that are not hydrolysed by lysosomal enzymes. The ultra-structural appearances of these cells in pregnant animals that 24-48h before had received intraperitoneal injections of Triton WR-1339, polyvinylpyrrolidone, dextran or sucrose revealed gross abnormalities that were confined to the vacuolar system; in comparison with normal tissue the number, and in some cases the size, of vacuoles was increased, leading to close packing within the apical cytoplasm and distortion of the normal rounded shape. By culturing yolk sacs in vitro, rates of ingestion of 125I-labelled polyvinylpyrrolidone and of 125I-labelled bovine serum albumin were determined, together with the rate of digestion of the labelled protein. The rates of exocytosis of 125I-labelled polyvinylpyrrolidone and of lysosomal enzymes were also determined. No significant differences between normal and highly vacuolated tissues were found. Apparently marked vacuolation of these cells by these agents is without significant effect on pinocytosis, exocytosis or intralysosomal proteolysis.  (+info)

Acetylglucosaminidase (ACG) is an enzyme that catalyzes the hydrolysis of N-acetyl-beta-D-glucosaminides, which are found in glycoproteins and glycolipids. This enzyme plays a crucial role in the degradation and recycling of these complex carbohydrates within the body.

Deficiency or malfunction of Acetylglucosaminidase can lead to various genetic disorders, such as mucolipidosis II (I-cell disease) and mucolipidosis III (pseudo-Hurler polydystrophy), which are characterized by the accumulation of glycoproteins and glycolipids in lysosomes, resulting in cellular dysfunction and progressive damage to multiple organs.

The enzyme α-N-acetylglucosaminidase (EC 3.2.1.50, α-acetylglucosaminidase, N-acetyl-α-D-glucosaminidase, N-acetyl-α- ... von Figura K (November 1977). "Human α-N-acetylglucosaminidase. 2. Activity towards natural substrates and multiple recognition ... Weissmann B, Rowin G, Marshall J, Friederici D (January 1967). "Mammalian α-acetylglucosaminidase. Enzymic properties, tissue ... von Figura K (November 1977). "Human α-N-acetylglucosaminidase. 1. Purification and properties". European Journal of ...
... is a protein that in humans is encoded by the ENGASE gene. This gene encodes a cytosolic ... "Entrez Gene: Endo-beta-N-acetylglucosaminidase". Retrieved 2018-08-24. Suzuki T, Yano K, Sugimoto S, Kitajima K, Lennarz WJ, ... Butkinaree C, Cheung WD, Park S, Park K, Barber M, Hart GW (August 2008). "Characterization of beta-N-acetylglucosaminidase ... Park K, Saudek CD, Hart GW (July 2010). "Increased expression of beta-N-acetylglucosaminidase in erythrocytes from individuals ...
In enzymology, a beta-aspartyl-N-acetylglucosaminidase (EC 3.2.2.11) is an enzyme that catalyzes the chemical reaction 1-beta- ... Eylar EH, Murakami M (1966). "beta-Aspartyl-N-acetylglucosaminidase from epididymis". Methods Enzymol. Methods in Enzymology. 8 ...
The enzyme N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase (EC 3.1.4.45) catalyzes the reaction glycoprotein N- ... Other names in common use include α-N-acetylglucosaminyl phosphodiesterase, lysosomal α-N-acetylglucosaminidase, phosphodiester ... glycosidase, α-N-acetyl-D-glucosamine-1-phosphodiester, N-acetylglucosaminidase, 2-acetamido-2-deoxy-α-D-glucose 1- ...
Further evidence of a hyperactive ?-N-acetylglucosaminidase-producing allele". Clinical Genetics. 41 (5): 243-247. doi:10.1111/ ...
These include: β-n-acetylglucosaminidase β-acetylaminodeoxyglucosidase β-acetamidodeoxyglucosidase β-acetylglucosaminidase n- ... Frohwein, Yaacov Zvi; Gatt, Shimon (1967-09-01). "Isolation of β-N-Acetylhexosaminidase, β-N-Acetylglucosaminidase, and β-N- ... Ueda, Mitsuhiro; Arai, Motoo (January 1992). "Purification and Some Properties ofβ-N-Acetylglucosaminidase fromAeromonassp. 10S ... IWAMOTO, Tooru; INAOKA, Megumu; NAKA, Hideyuki (1983). "Mycelial .BETA.-N-acetylglucosaminidase of Streptomyces sp. having . ...
N-acetylglucosaminidase, alpha is a protein that in humans is encoded by the NAGLU gene. This gene encodes an enzyme that ... "Entrez Gene: N-acetylglucosaminidase, alpha". Weber B, Blanch L, Clements PR, Scott HS, Hopwood JJ (June 1996). "Cloning and ... "Purification and partial characterization of alpha-N-acetylglucosaminidase from human liver". Journal of Biochemistry. 110 (5 ...
... alpha-N-acetylglucosaminidase (type B; MIM 252920); acetyl CoA:alpha-glucosaminide acetyltransferase (type C; MIM 252930); and ...
Chien S, Weinburg R, Li S, Li Y (1977). "Endo-β-N-acetylglucosaminidase from fig latex". Biochem. Biophys. Res. Commun. 76: 317 ... doi:10.1016/0006-291x(77)90727-6. Koide N, Muramatsu T (August 1974). "Endo-β-N-acetylglucosaminidase acting on carbohydrate ... The enzyme mannosyl-glycoprotein endo-β-N-acetylglucosaminidase (endoglycosidase H) (EC 3.2.1.96) has systematic name ... "Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity". The Journal ...
N-Acetylglucosaminidase: Experimentally found within mouse cortical granules, N-Acetylglucosaminidase is a glycosidase that ... Therefore, N-Acetylglucosaminidase contributes to polyspermy prevention. p32: The name, p32, refers to the protein's molecular ...
N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase is an enzyme that in humans is encoded by the NAGPA gene. ... "Entrez Gene: NAGPA N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase". Lee, W. S.; Kang, C.; Drayna, D.; ... "Purification and characterization of human serum N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase". Arch. ... "Purification and characterization of human lymphoblast N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase". ...
Brunner K, Peterbauer CK, Mach RL, Lorito M, Zeilinger S, Kubicek CP (July 2003). "The Nag1 N-acetylglucosaminidase of ... Chitinases (EC 3.2.1.14, chitodextrinase, 1,4-β-poly-N-acetylglucosaminidase, poly-β-glucosaminidase, β-1,4-poly-N-acetyl ... The regulation of an endochitinase in Trichoderma atroviride is dependent on a N-acetylglucosaminidase, and the data indicates ... Family 20 includes N-acetylglucosaminidase and a similar enzyme, N-acetylhexosaminidase. And as the gene sequences of the ...
"Purification and Multimeric Structure of BovineN-Acetylglucosamine-1-phosphodiester α-N-Acetylglucosaminidase *". Journal of ... and functional expression of two splice forms of human N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase". J ... include defining the structure and function of N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase, commonly ...
... produces endo-β-N-acetylglucosaminidase mithramycin, amicetin, bamicetin, and plicacetin. Kanini, ... "High-level expression of endo-β-N-acetylglucosaminidase H from Streptomyces plicatus in Pichia pastoris and its application for ...
Sanfilippo B is caused by the missing or deficient enzyme alpha-N-acetylglucosaminidase. Sanfilippo C results from the missing ...
Membrane-bound β-N-Acetylglucosaminidase Probably Involved in the Processing of Protein N-Glycans". Journal of Biological ... "The Drosophila fused lobes Gene Encodes an N-Acetylglucosaminidase Involved in N-Glycan Processing". Journal of Biological ... "Improvement of glycosylation structure by suppression of β-N-acetylglucosaminidases in silkworm". Journal of Bioscience and ...
... cytosolic beta-N-acetylglucosaminidase from human brain". The Journal of Biological Chemistry. 276 (13): 9838-45. doi:10.1074/ ... cytosolic beta-N-acetylglucosaminidase from human brain". The Journal of Biological Chemistry. 276 (13): 9838-45. doi:10.1074/ ... "Analysis of MGEA5 on 10q24.1-q24.3 encoding the beta-O-linked N-acetylglucosaminidase as a candidate gene for type 2 diabetes ... further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase". The Journal of Biological ...
Frohwein YZ, Gatt S (September 1967). "Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N- ...
Tachibana Y, Yamashita K, Kobata A (1982). "Substrate specificity of mammalian endo-beta-N-acetylglucosaminidase: study with ...
Alpha-N-acetylglucosaminidase is a lysosomal enzyme required for the stepwise degradation of heparan sulphate. Mutations on the ... Glycoside hydrolase family 89 CAZY GH_89 includes enzymes with α-N-acetylglucosaminidase EC 3.2.1.50 activity. The enzyme ... "Mouse model of Sanfilippo syndrome type B produced by targeted disruption of the gene encoding alpha-N-acetylglucosaminidase". ... alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B ...
Frohwein YZ, Gatt S (September 1967). "Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N- ... cytosolic beta-N-acetylglucosaminidase from human brain". J. Biol. Chem. 276 (13): 9838-45. doi:10.1074/jbc.M010420200. PMID ... β-N-acetylglucosaminidase, hexosaminidase A, N-acetylhexosaminidase, β-D-hexosaminidase) is an enzyme involved in the ... for β-N-acetylglucosaminidase, β-N-acetylhexosaminidase and β-N-acetylgalactosaminidase". Biochem. J. 261 (3): 1059-60. doi: ...
Functionally, five types of lysin catalytic domain can be distinguished: Endo-β-N-acetylglucosaminidase (Endoglycosidase H, EC ... Endo-β-N-acetylglucosaminidase lysins cleave NAGs while N-acetylmuramidase lysins (lysozyme-like lysins) cleave NAMs. ...
... CAZY GH_73 includes peptidoglycan hydrolases with endo-β-N-acetylglucosaminidase specificity. ...
"The structure of hyperthermophilic β-N-acetylglucosaminidase reveals a novel dimer architecture associated with the active site ...
... enzymes have endo-beta-N-acetylglucosaminidase activity EC 3.2.1.96 (CAZY GH_85). These enzymes ...
"The Nag1 N-acetylglucosaminidase of Trichoderma atroviride is essential for chitinase induction by chitin and of major ...
... and β-N-acetylglucosaminidase. Shell membrane is mainly used as a dietary supplement in a partially hydrolyzed powder form. " ...
β-N-Acetylglucosaminidase (from Streptococcus pneumoniae): cleaves all non-reducing terminal β-linked N-acetylglucosamine ...
... produces secalonic acid D, chitinase, oxalic acid, oxaline and β-N-acetylglucosaminidase and occurs ...
CBM32 modules are associated with catalytic modules such as sialidases, B-N-acetylglucosaminidases, α-N-acetylglucosaminidases ...
The enzyme α-N-acetylglucosaminidase (EC 3.2.1.50, α-acetylglucosaminidase, N-acetyl-α-D-glucosaminidase, N-acetyl-α- ... von Figura K (November 1977). "Human α-N-acetylglucosaminidase. 2. Activity towards natural substrates and multiple recognition ... Weissmann B, Rowin G, Marshall J, Friederici D (January 1967). "Mammalian α-acetylglucosaminidase. Enzymic properties, tissue ... von Figura K (November 1977). "Human α-N-acetylglucosaminidase. 1. Purification and properties". European Journal of ...
ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H
It is a peptidoglycan hydrolase with endo-β-N-acetylglucosaminidase specificity. The recombinant CdAcp73A, purified from ... "β-Acetylglucosaminidase 73A (CdAcp73A), assigned the E.C. number 3.2.1.-, is a derivative of Clostridium difficile. ... β-Acetylglucosaminidase 73A (CdAcp73A), assigned the E.C. number 3.2.1.-, is a derivative of Clostridium difficile. It is a ... β-Acetylglucosaminidase 73A (CdAcp73A), assigned the E.C. number 3.2.1.-, is a derivative of Clostridium difficile. It is a ...
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase*Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase ... Analysis of cholecystokinin-binding proteins using endo-beta-N-acetylglucosaminidase F. J Cell Biol. 1984 Sep; 99(3):1110-6. ... This graph shows the total number of publications written about "Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase" by ... Below are the most recent publications written about "Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase" by people in ...
N-acetyl-glucosaminidase (NAG). NAG is an enzyme found predominantly in lysosomes of the proximal tubular cells and has ...
Impact of peptidoglycan O-acetylation on autolytic activities of the Enterococcus faecalis N-acetylglucosaminidase AtlA and N- ... the N-acetylglucosaminidase AtlA and the N-acetylmuramidase AtlB. We constructed isogenic strains with various O-acetylation ...
Endo-Beta-N-Acetylglucosaminidase H, D130N/E132Q Double Mutant ... ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H: A. SMTL:PDB. SMTL Chain Id ... Endo-Beta-N-Acetylglucosaminidase H, D130N/E132Q Double Mutant Coordinates. PDB Format Method. X-RAY DIFFRACTION 2.10 Å. Oligo ... Rao, V. et al., Mutations of endo-beta-N-acetylglucosaminidase H active site residues Asp130 and Glu132: activities and ...
N-acetylglucosaminidase. +. +. Acid phosphatase. -. -. Alkaline phosphatase. -. -. Pyrrolidonylarylamidase. -. -. API Strep ...
In Pakistan, milk quality control standards are yet to be established. The prime objective of this study was to develop the standard referencevalues for the milk pH, its somatic cell count (SCC), electric conductivity (EC) and NAGase i.e., milk enzyme in the noninfected milk of localbuffalo breed i.e., Nilli-Ravi also known as Black-gold of Pakistan and cows i.e., Sahiwal and other crossbred cows kept locally mostly formilch purpose. A total of 30 animals with lactation number 1-5 (in early lactation of two months) from each breed group were selectedfor milk samples. Samples were then tested for mastitis through Surf Field Mastitis test and microbiological culturing. Reference valueswere determined using negative samples. Fore-mentioned parameters were analyzed for collected Milk samples. The values for NAGaseand SCC were the most eminent in the crossbred cows milk i.e., (56.07±2.33 U/mL) & (178645.83±2324.0/mL) respectively. EC value(5.7±0.04) was strikingly high in Sahiwal cows milk. Milk of
Endo-β-N-acetylglucosaminidase H; ER, endoplasmic reticulum; ESI-MS, electrospray ionization mass spectrometry; GST, ...
... subclinical effects such as significant increases in mean levels of urinary tubular enzymes alanine-aminopeptidase and N-acetyl- glucosaminidase ... n-acetyl glucosaminidase; NAGA; alanine aminopeptidase; AAP ...
... a soluble exo-beta-D-galactosidase and a soluble exo-beta-D-N-acetylglucosaminidase. The endoglycosidases were shown to act ... The particulate endoglycosidase and the soluble exo-beta-D-galactosidase and exo-beta-D-N-acetylglucosaminidase are induced ... a soluble exo-beta-D-galactosidase and a soluble exo-beta-D-N-acetylglucosaminidase. The endoglycosidases were shown to act ...
endo-β-N-Acetylglucosaminidase (= Endo-M). Recombinant: from Mucor hiemalis expressed in Candida boidinii [Purity: single band ...
1 Quantification of Lysosomal Membrane Permeabilization by Cytosolic Cathepsin and b-N-Acetyl-Glucosaminidase Activity ...
Endo-beta-Acetylglucosaminidase Endo-beta-N-Acetylglucosaminidase D Endo-beta-N-Acetylglucosaminidase F Endo-beta-N- ... Endo-beta-N-Acetylglucosaminidase H Narrower Concept UI. M0009336. Registry Number. EC 3.2.1.96. Terms. Endo-beta-N- ... Endo-beta-N-Acetylglucosaminidase D Narrower Concept UI. M0025886. Registry Number. EC 3.2.1.96. Terms. Endo-beta-N- ... Endo-beta-N-Acetylglucosaminidase F Narrower Concept UI. M0009335. Registry Number. EC 3.2.1.96. Terms. Endo-beta-N- ...
Theantana T., Chantawannakul P. (2008) Protease and beta-N-acetylglucosaminidase of honey bee chalkbrood pathogen Ascosphaera ...
Endo-beta-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cells. ...
Glycoside hydrolase family GH85 is a family of endo-β-N-acetylglucosaminidases that is responsible for the hydrolysis of β-1,4 ... The X-ray Crystal Structure of an Arthrobacter protophormiae Endo-β-N-Acetylglucosaminidase Reveals a (β/α)8 Catalytic Domain, ... The X-ray Crystal Structure of an Arthrobacter protophormiae Endo-β-N-Acetylglucosaminidase Reveals a (β/α)8 Catalytic Domain, ... The endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae (Endo-A) is of particular interest, given its increasing use ...
... beta-n-acetyl glucosaminidase release, and cytotoxicity as measured by trypan blue dye exclusion. It is important to note that ...
... ß-acetylglucosaminidase and proteinase during the first 28 days, with recovery after 2 months; no effect was observed at 0.1 mg ...
β-N-acetylglucosaminidase was determined using the reaction mixture contained 100 μL p-nitrophenyl-N-acetylglucosaminide (5 mM ... One unit of β-N-acetylglucosaminidase activity was defined as the amount of enzyme necessary to liberate 1 μmol p-nitrophenol ... According to these results, the chitinase did not have β-N-acetylglucosaminidase activity but had endochitinase activity as it ...
N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide beta -1,4-N-acetylglucosaminidase. ... N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide beta -1,4-N-acetylglucosaminidase ...
The activities of β-N-acetylglucosaminidase, β-galactosidase and β-glycosidase in the former were distinguished from those in ...
N-acetyl-glucosaminidase (NAG). NAG, which is an enzyme found predominantly in lysosomes of the proximal tubular cells, has ...
Potential activities of two enzymes related to soil N cycling - β-N-acetylglucosaminidase (NAG) associated with chitin and ... 2d), although ECM-dominated plots had high potential β-N-acetylglucosaminidase activities (Fig. 4c). The decoupling between N- ... N-acetylglucosaminidase activities. These shifts in soil microbial abundances and enzyme activities along the mycorrhizal ...
Alpha-N-acetylglucosaminidase. *Morquio syndrome B (MPS IV B). *Beta-galactosidase. *Maroteaux-Lamy syndrome (MPS VI). ...
suchlasporia TAMA 87 as a potent β-N-acetylglucosaminidase inhibitor. Usuki, H., Toyo-oka, M., Kanzaki, H., Okuda, T. & Nitoda ... Screening and partial characterization of inhibitors of insect β-N-acetylglucosaminidase. Usuki, H., Nitoda, T., Okuda, T. & ... New analogs of pochonicine, a potent β-N-acetylglucosaminidase inhibitor from fungus Pochonia suchlasporia var. suchlasporia ... TMG-chitotriomycin, an enzyme inhibitor specific for insect and fungal β-N-acetylglucosaminidases, produced by actinomycete ...
Serum assays for lysosomal enzymes (alpha-L-iduronidase, iduronate sulfatase, heparan N-sulfatase, N-acetylglucosaminidase, ...
This is Pfanness personal scorecard. Here you can view all their essential playing statistics and history, including the number of individual records and awards they currently hold on Wordtwist. These stats are updated in real-time, so check back often to keep track of Pfanness progress. ...
... an α-N-acetylglucosaminidase (GH89), an α-amylase (GH13), a galactosidase (GH43) and a β-hexosaminidase (GH20) (Davey et al. ...
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (musc.edu)
  • This graph shows the total number of publications written about "Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase" by people in this website by year, and whether "Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase" was a major or minor topic of these publications. (musc.edu)
  • Below are the most recent publications written about "Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase" by people in Profiles. (musc.edu)
  • Analysis of cholecystokinin-binding proteins using endo-beta-N-acetylglucosaminidase F. J Cell Biol. (musc.edu)
  • Mutations of endo-beta-N-acetylglucosaminidase H active site residues Asp130 and Glu132: activities and conformations. (expasy.org)
  • Huang C, Harada Y, Hosomi A, Masahara-Negishi Y, Seino J, Fujihira H, Funakoshi Y, Suzuki T, Dohmae N, Suzuki T. Endo-beta-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cells. (medlineplus.gov)
  • The ECM tree dominance was negatively related to soil bacterial and AOA amoA gene abundances, and positively to soil fungal abundances and β- N -acetylglucosaminidase activities. (researchsquare.com)
  • The particulate endoglycosidase and the soluble exo-beta-D-galactosidase and exo-beta-D-N-acetylglucosaminidase are induced when the bacteria is grown in adaptative media containing either 0.1% keratan sulfate or 0.1% chondroitin sulfate. (nih.gov)
  • The enzyme α-N-acetylglucosaminidase (EC 3.2.1.50, α-acetylglucosaminidase, N-acetyl-α-D-glucosaminidase, N-acetyl-α-glucosaminidase, α-D-2-acetamido-2-deoxyglucosidase) is a protein associated with Sanfilippo syndrome, with systematic name α-N-acetyl-D-glucosaminide N-acetylglucosaminohydrolase. (wikipedia.org)
  • Structural characterization of the α-N-acetylglucosaminidase, a key enzyme in the pathogenesis of Sanfilippo syndrome B". Journal of Structural Biology. (wikipedia.org)
  • Glycoside hydrolase family GH85 is a family of endo-β-N-acetylglucosaminidases that is responsible for the hydrolysis of β-1,4 linkage in the N,N-diacetylchitobiose core of N-linked glycans. (hud.ac.uk)
  • Mouse model of Sanfilippo syndrome type B produced by targeted disruption of the gene encoding alpha -N-acetylglucosaminidase. (nih.gov)
  • At 2 ppm, injury was marked by significant increases in BALF total protein, N -acetylglucosaminidase, and lavageable ciliated cells. (nih.gov)
  • Excretion of creatinine, phosphorus, protein, N-acetylglucosaminidase (NAG), and the major metabolite of DCP, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC), was measured. (nih.gov)
  • Alpha-N-acetylglucosaminidase removes a sugar called N-acetylglucosamine when it is at the end of the GAG chain. (medlineplus.gov)
  • The beta- N -acetylglucosaminidase removes terminal N -acetyl-D-glucosamine from the GlcNAcbeta1, 2Manalpha1,3Manbeta- arm of Manalpha1,6(GlcNAcbeta1,2Manalpha1,3) Manbeta1,4GlcNAcbeta1,4GlcNAc-R to produce paucimannose Man(3)GlcNAc(2) N-glycan. (nih.gov)
  • The lack of alpha-N-acetylglucosaminidase activity disrupts the breakdown of a subset of GAGs called heparan sulfate. (medlineplus.gov)
  • Unfortunately, progress in structure-activity studies of keratan sulfate (KS) have been impeded by the lack of a commercially available endo-β-N-acetylglucosaminidase, keratantase II. (rpi.edu)