Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Jan Stockx"'
Autor:
Ignace Debruyne, Jan Stockx
Publikováno v:
Enzyme. 23:361-372
Hen's egg white and vitelline membrane nucleoside triphosphatases were purified resulting in active soluble subunits with MR 260,000 +/- 10,000. PH optima are divalent cation dependent and situated at pH 6.2 and 8.0 with ATP and at pH 6.15 with ADP a
Autor:
Jan Stockx, Ignace Debruyne
Publikováno v:
Biochemical Society Transactions. 5:1109-1111
Autor:
Jan Stockx, Jan Wouters
Publikováno v:
Biochemical Society Transactions. 5:1104-1106
Publikováno v:
The International journal of biochemistry. 17(3)
Two acid proteases from the yolk and one from the yolk-sac of the hen's egg were purified and characterized. They belong all three to the class of cathepsin D. Mostly, minor differences were found in their properties. Possible endogenous substrates,
Autor:
Ignace Debruyne, Jan Stockx
Publikováno v:
The International journal of biochemistry. 10(12)
1. 1. Alkaline phosphatases from hen's egg yolk, liver, blood plasm, and intestinal mucosa were purified with, as main purification step, affinity chromatography on 4-(p-amino-phenylazo)-phenylarsonic acid-epoxy-Sepharose 4B. Specific activities up t
Publikováno v:
Biochimica et biophysica acta. 614(2)
The cholinesterase (acylcholine acylkhydrolase, EC 3.1.1.8) of chicken egg yolk was partly purified and characterized. It was compared to homologous enzymes of liver and blood plasma of laying hens. During gel filtration, yolk and liver cholinesteras
Autor:
Jan Stockx, Stefaan de Boeck
Publikováno v:
The International journal of biochemistry. 18(7)
Lysozyme accounts for 37% of the proteins of the hen's egg vitelline membrane. It can be extracted by salt solutions and purified by gel filtration on Sephadex G-50. There are no differences between the chemical and enzymic properties of egg white an
Publikováno v:
European journal of biochemistry. 52(1)
Chicken egg yolk contains an adenosine deaminase that was investigated after purifying about 500 times. It has a pH optimum at 6.5, aKm of 6.6 times 10(-5) mol/l and an approximate molecular weight of 14000; higher molecular forms could not be detect
Autor:
Jan Stockx, Stefaan de Boeck
Publikováno v:
The International journal of biochemistry. 18(7)
1. 1. Salt solutions and charged detergents are efficient solubilising agents for ovovitelline membrane lysozyme. 2. 2. Reassociation experiments with chemically modified lysozymes indicate that positively charged amino acid residues of lysozyme (the
Autor:
Jan Stockx, Jan Wouters
Publikováno v:
Archives Internationales de Physiologie et de Biochimie. 85:1037-1038