Analysis of Mixtures of Glucosamine and Galactosamine with Bakers' Yeast

Pogell, Burton M.; Koenig, D. F.

doi:10.1038/182127a0

Cited by 12 publications

(10 citation statements)

References 9 publications

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“…Effect of variou-s compounds on enzyme activity. In view of the relationship between the reaction catalysed by pyridoxamine phosphate oxidase and those reactions catalysed by monoamine oxidase and diamine oxidase (Pogell, 1958;Zeller, 1951), and evidence that the oxidations of pyridoxamine phosphate and pyridoxine phosphate to pyridoxal phosphate are catalysed by a single protein (Wada & Snell, 1961), the effects of iproniazid, isoniazid and amines as indicated below on pyridoxine phosphate oxidase were investigated.…”

Section: Resultsmentioning

confidence: 99%

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THE CONVERSION OF PYRIDOXINE PHOSPHATE INTO PYRIDOXAL PHOSPHATE IN ESCHERICHIA COLI

Hm¹

1965

Biochemical Journal

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1. Evidence is presented for the presence of pyridoxine phosphate oxidase in aqueous extracts of Escherichia coli. Some comparison is made with pyridoxamine phosphate oxidase. 2. Isoniazid and iproniazid were found to combine with pyridoxal phosphate, but isoniazid did not combine with either pyridoxamine phosphate or pyridoxine phosphate. Both oxidase activities were somewhat inhibited by benzylamine and putrescine, but not by phenethylamine or cadaverine. 3. The significance of pyridoxine phosphate oxidase in cell metabolism is discussed.

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Section: Resultsmentioning

confidence: 99%

“…The enzymic oxidation of pyridoxamine phosphate to pyridoxal phosphate was demonstrated by Pogell (1958Pogell ( , 1963 in mammalian liver preparations. Beechey & Happold (1957) demonstrated the conversion of pyridoxamine phosphate into pyridoxal phosphate by an enzyme present in crude extracts of apotryptophanase from Escherichia coli.…”

mentioning

confidence: 98%

THE CONVERSION OF PYRIDOXINE PHOSPHATE INTO PYRIDOXAL PHOSPHATE IN ESCHERICHIA COLI

Hm¹

1965

Biochemical Journal

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“…20 ) The latter enzyme resembles PMP (PNP) oxidase in catalytic properties because L-a-amino acid as well as a-hydroxy acid can be oxidized by one enzyme protein. 21) PMP (PNP) oxidase was found in microbes,22) animals 23 ) and higher plants, 24) As to the yeast enzyme, the unusual subunit structure might reflect changeable catalytic properties, especially, on the relative substrate specificity against two naturally occurring substrates, PMP and PNP (ref. 2 and unpublished results).…”

Section: Preparation Of Apoenzymementioning

confidence: 99%

Molecular and Enzymatic Properties of Pyridoxamine (Pyridoxine) 5′-Phosphate Oxidase from Baker’s Yeast

Tsuge

Ozeki

Ohashi

1980

Agricultural and Biological Chemistry

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“…The peaks of radioactive material from each of three chromatographic analyses were freeze-dried. Glucosamine and galactosamine analyses (Neuhaus & Letzring, 1957;Pogell & Koenig, 1958) were made on a portion of the freeze-dried material which had been heated in 3N-HCI for 8hr. at 1100 in a sealed tube.…”

Section: Isolation Of Corium Embryonated Eggs From Kimber 137mentioning

confidence: 99%

Incorporation of sulphate by chick-embryo corium. Nature and products of the process in vitro

Noble

Boucek

1965

Biochemical Journal

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1. The incorporation of sulphate into the trichloroacetic acid-precipitable fraction of 9-day chick-embryo corium, incubated in Krebs-Ringer phosphate buffer, pH7, is dependent on the sulphate concentration of the medium. Uptake of sulphate is linear with time for 3.5-4hr. and is maximal at 37.5 degrees in the presence of air or oxygen. d-Glucose stimulates the incorporation of sulphate but l-glutamine has no effect. 2. Incorporation of sulphate by the chick corium is enzymic and apparently involves the synthesis of active sulphate (adenosine 3'-phosphate 5'-sulphatophosphate) and the transfer of sulphate from adenosine 3'-phosphate 5'-sulphatophosphate to acceptor glycosaminoglycuronoglycan. This proposal on the nature of the process is suggested by the similarity between the energy of activation calculated for sulphate-incorporation in the chick-corium preparation and the energy requirement reported for sulphate-activation with purified yeast enzymes. 3. The 9-day chick-embryo corium is composed principally of fibroblasts; there are no histologically demonstrable mast cells. The young fibroblast is apparently responsible for the incorporation of sulphate into glycosaminoglycuronoglycans tentatively identified as chondroitin sulphate(s), heparan sulphate and heparin-like material.

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Analysis of Mixtures of Glucosamine and Galactosamine with Bakers' Yeast

Cited by 12 publications

References 9 publications

THE CONVERSION OF PYRIDOXINE PHOSPHATE INTO PYRIDOXAL PHOSPHATE IN ESCHERICHIA COLI

THE CONVERSION OF PYRIDOXINE PHOSPHATE INTO PYRIDOXAL PHOSPHATE IN ESCHERICHIA COLI

Molecular and Enzymatic Properties of Pyridoxamine (Pyridoxine) 5′-Phosphate Oxidase from Baker’s Yeast

Incorporation of sulphate by chick-embryo corium. Nature and products of the process in vitro

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