Ophion luteus

DNA-relaxing enzyme from Micrococcus luteus.

A DNA-relaxing enzyme which catalyzes the conversion of superhelical DNA to a non-superhelical covalently closed form has been purified from Micrococcus luteus to near homogeneity by two chromatographic steps. The enzyme is a single polypeptide chain. As determined by sodium dodecyl sulfate - polyacrylamide gel electrophoresis and gel filtration on Sephadex G 150, the molecular weight is 115,00...

Binding of Dissolved Strontium by Micrococcus luteus.

Resting cells of Micrococcus luteus have been shown to remove strontium (Sr) from dilute aqueous solutions of SrCl(2) at pH 7. Loadings of 25 mg of Sr per g of cell dry weight were achieved by cells exposed to a solution containing 50 ppm (mg/liter) of Sr. Sr binding occurred in the absence of nutrients and did not require metabolic activity. Initial binding was quite rapid (<0.5 h), although a...

A mutable luteus locus in maize

مطالعه فونستیک زنبورهای خانواده‌ Ichneumonidae در استان یزد

فون زنبور­های خانواده‌ Ichneumonidaeدر شهرستان یزد و مناطق اطراف در سال‌های 1385 تا 1387 مورد بررسی قرار گرفت. بر اساس نتایج به ­دست آمده 8 گونه به ­شرح زیر جمع­ آوری و شناسایی گردید. بر اساس منابع موجود، دو گونه که با ستاره مشخص شده­اند برای اولین ­بار از ایران گزارش می شوند. 1. Diplazon laetatorius (Fabricius, 1781) 2. Ophion ventricosus Gravenhorst, 1829 3. Ophion luteus (Linnaeus, 1758)*...

Biochemical properties of penicillin amidohydrolase from Micrococcus luteus.

Some biochemical properties of whole-cell penicillin amidohydrolase from Micrococcus luteus have been studied. This whole-cell enzyme showed its maximal activity at 36 degrees C at pH 7.5. It was found that the activation energy of this enzyme was 8.03 kcal (ca. 33.6 kJ) per mol, and this amidohydrolase showed first-order decay at 36 degrees C. The penicillin amidohydrolase was deactivated rapi...