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M Elander

Publications and source records attributed to M Elander.

3 recordsLinked to original sources

Bovine serum chitinase.

1. A glycol-chitin-splitting enzyme without lysozyme (muramidase) activity has been found in calf serum. The enzyme also degrades colloidal chitin and is thus a true chitinase, 1,4-beta-poly-N-acetylglucosaminidase, without exo-beta-N-acetylglucosaminidase effect. 2. The enzyme is purified 1000-fold by ion-exchange chromatography and gel filtration. Its optimal activity is between pH 1.5-2.0 with glycol chitin and between pH 3-6 in a rather broad optimum with colloidal chitin as substrate. The optimal stability of the enzyme is in the pH interval 3.0-6.5 when tested by incubation with glycol chitin at 50 degrees C for 60 min. The optimal temperature for the degradation of glycol chitin is 40 degrees C when assayed at pH 1.5 and 51 degrees C when assayed at pH 3.5. 3. The enzyme is activated by moderate heating at pH 6.5. The highest relative activity, 135% is reached after 45 min incubation at 30 degrees C, pH 5 or after 30 min at 40, pH 2.4. By incubation with small amounts of trypsin at pH 6.5 at 3m degrees C the enzyme was temporarily activated. 4. The isoelectric point, pH 5.3, and the molecular weight, 47,000 +/- 3,000 were determined by respectively isoelectric focusing and gel filtration. 5. The Michaelis-Menten constant, Km = 0.76 +/- 0.05 (S.E.) mg/ml, was measured with glycol chitin as substrate.

Animals

Mass fragmentographic determination of diphenylhydantoin and its main metabolite, 5-(4-hydroxyphenyl)-5-phenylhydantoin, in human plasma.

A method is described for the mass fragmentographic determination of diphenylhydantoin and its main metabolite, 5-(-4-hydroxyphenyl)-5-phenylhydantoin (4-OH-DPH), in human plasma as their dimethyl and trimethyl derivatives, respectively. The derivatives are formed by using the recently described extractive alkylation technique. Pentadeuterated 4-OH-DPH is used as the internal standard. Following acidic hydrolysis of the plasma sample, conjugated 4-OH-DPH and, indirectly, the dihydrodiol metabolite, 5-(3,4-dihydroxy-1,5-cyclohexadien-1-yl)-5-phenylhydantoin, are measured. Using 100-mul plasma samples, the lower limit of detection is about 10 ng/ml 00.03 nmole/ml).

Alkylation

Chitinase and beta-N-acetylglycosaminidase in the digestive juice of Helix pomatia.

A beta-N-acetylglucosaminidase from Helix pomatia digestive juice was separated and partly purified by gel chromatography. The optimal pH for the degradation of p-nitrophenyl-N-acetyl-beta-D-glucosaminide was 3.4. The molecular weight was around 160 000 and the pI = 4.95. In the same gel chromatography run two chitinase active peaks were also obtained. These chitinase active peaks were also obtained. These chitinases, with molecular weights around 26 000 and 13 000, had somewhat different pH activity curves with optima at 4.2 and 4.3. By isoelectric focusing the first peak with molecular weight around 26 000 was divided in two chitinase active regions with pI at 5.7 and 3.5. The second peak with molecular weight around 13 000 had a pI at 7.3.

Acetylglucosaminidase