Separation of and from calf brain cytoplasm

Frohwein, Yaacov Zvi; Gátt, Shimon

doi:10.1016/0926-6593(66)90167-6

Cited by 36 publications

(5 citation statements)

References 6 publications

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“…A recent report of multiple forms of N-acetyl-,glucosaminidase in calf brain reopens the question of specificity. Frohwein & Gatt (1966) found a particulate enzyme with both glucosaminidase and galactosaminidase activity and also two C-4specific supernatant enzymes. The last two enzymes were obtained by having present either dithiothreitol or N-ethylmaleimide during the extraction, and it is possible that the substrate-binding activity of a single species may have been altered by the presence of one or other of these reagents to give the semblance of two distinct forms.…”

Section: Purification Step Spleen Supernatant Extractmentioning

confidence: 93%

N-Acetyl-β-glucosaminidases in human spleen

Robinson

Stirling

1968

Biochemical Journal

502

136

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1. The N-acetyl-beta-glucosaminidase of human spleen has been separated by gel electrophoresis into two components, an acidic form A and a basic form B. 2. The two forms are readily separated on DEAE-cellulose and have been concentrated 50-fold and sevenfold respectively. 3. They show similar K(m) values towards 4-methylumbelliferyl N-acetyl-beta-d-glucosaminide, and have the same pH optima when compared in citrate, phosphate or acetate buffers. They are inhibited to a similar extent by acetate, heparin, N-acetylgalactosaminolactone, N-acetyl-beta-d-galactosamine and N-acetyl-beta-d-glucosamine. Specificity for C-4 orientation is not absolute and p-nitrophenyl beta-galactosaminide is also hydrolysed but at a rate only 11.6% of that for the corresponding glucosaminide. 4. N-Acetyl-beta-glucosaminidase B is stable over a wider pH range than is N-acetyl-beta-glucosaminidase A, and is less easily denatured by heat. 5. Tissue fractionation indicates that both the A and B forms are present in the lysosomal fraction, whereas the supernatant contains the A form only. 6. Evidence is presented to indicate that the A form contains a number of sialic acid residues.

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Section: Purification Step Spleen Supernatant Extractmentioning

confidence: 93%

N-Acetyl-β-glucosaminidases in human spleen

Robinson

Stirling

1968

Biochemical Journal

502

136

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“…p-Nitrophenyl /3-glycopyranosides were used to determine /3-glycosidase activity (glucosidase, galactosidase, jV-acetylglucosaminidase, and JV-acetylgalactosaminidase). The following modification of the method of Frohwein and Gatt (1966) was used for glucosidase and galactosidase: 0.5 µ of substrate and 50 /mióles of potassium acetate buffer (pH 5.0); and for hexosaminidases : 0.4 µ ß of substrate and sodium citrate buffer.…”

Section: Methodsmentioning

confidence: 99%

Human brain sialidase

Öhman¹,

Rosenberg²,

Svennerholm³

1970

Biochemistry

114

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“…Although it appears that N-acetylgalactosaminidase activity is always associated with N-acetylglucosaminidase activity, the converse does not appear to be so, since an enzyme has been prepared from calf brain which catalyses N-acetylgalactosaminidase activity but not N-acetylglucosaminidase activity (Frohwein & Gatt, 1966).…”

Section: Resultsmentioning

confidence: 97%

Immunological evidence to show that the N-acetylglucosaminidase and N-acetylgalactosaminidase activities of Dictyostelium discoideum reside in the same protein molecule (Short Communication)

Every

Ashworth

1974

Biochemical Journal

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Antibodies were produced against purified beta-N-acetylhexosaminidase from Dictyostelium discoideum. Ouchterlony tests produced a single precipitin band with both beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase activities. Both activities were co-precipitated in exactly the same proportions in quantitative immunoprecipitation reactions. We conclude that one enzyme protein catalyses the hydrolysis of both N-acetylglucosaminides and N-acetylgalactosaminides.

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Separation of and from calf brain cytoplasm

Cited by 36 publications

References 6 publications

N-Acetyl-β-glucosaminidases in human spleen

N-Acetyl-β-glucosaminidases in human spleen

Human brain sialidase

Immunological evidence to show that the N-acetylglucosaminidase and N-acetylgalactosaminidase activities of Dictyostelium discoideum reside in the same protein molecule (Short Communication)

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