Presence of conjugase activity in amethopterin-resistant Streptococcus faecium.
نویسندگان
چکیده
منابع مشابه
Folate reductase and specific dihydrofolate reductase activities of the amethopterin-sensitive Streptococcus faecium var. durans.
Preliminary evidence is presented that indicates that the dihydrofolate reductase activity of amethopterin-sensitive Streptococcus faecium var. durans ATCC 8043 is separable into two dihydrofolate reductases, one of which also reduces folate.
متن کاملDihydrofolate Reductase of Streptococcus f aecium II. PURIFICATION AND SOME PROPERTIES OF TWO DIHYDROFOLATE REDUCTASES FROM THE AMETHOPTERIN-RESISTANT
From a single amethopterin-resistant organism, Streptococcus faecium var. durans strain A, two different dihydrofolate reductases have been obtained as essentially homogeneous proteins in good yield. One of the reductases has a similar substrate specificity and turnover number (about 8000 moles per min per mole of enzyme) to the single reductase found in the amethopterin-sensitive strain of S. ...
متن کاملDihydrofolate Reductase of Streptococcus f aecium
From a single amethopterin-resistant organism, Streptococcus faecium var. durans strain A, two different dihydrofolate reductases have been obtained as essentially homogeneous proteins in good yield. One of the reductases has a similar substrate specificity and turnover number (about 8000 moles per min per mole of enzyme) to the single reductase found in the amethopterin-sensitive strain of S. ...
متن کاملDihydrofolate reductase from amethopterin-resistant Lactobacillus casei. Sequences of the cyanogen bromide peptides and complete sequences of the enzyme.
The complete amino acid sequence of dihydrofolate reductase from an amethopterin-resistant strain of Lactobacillus casei has been determined by sequence analysis of peptides produced by cleavage with cyanogen bromide, trypsin, staphylococcal protease, and myxobacter protease. Comparison of this sequence with those of reductases from other bacterial sources shows that the enzymes are homologous....
متن کاملDihydrofolate Reductase from Amethopterin-resistant Lactobacillus casei SEQUENCES OF THE CYANOGEN BROMIDE PEPTIDES AND COMPLETE SEQUENCE OF THE ENZYME*
The complete amino acid sequence of dihydrofolate reductase from an amethopterin-resistant strain of Lactobacillus casei has been determined by sequence analysis of peptides produced by cleavage with cyanogen bromide, trypsin, staphylococcal protease, and myxobatter protease. Comparison of this sequence with those of reductases from other bacterial sources shows that the enzymes are homologous....
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of bacteriology
دوره 95 6 شماره
صفحات -
تاریخ انتشار 1968