The Presence of an Exonuclease in Highly Purified DNA Polymerase from Bakers' Yeast
نویسندگان
چکیده
منابع مشابه
DNA polymerases from bakers' yeast.
Two DNA polymerases are present in extracts of commercial bakers' yeast and wild type Saccharomyces cerevisiae grown aerobically to late log phase. Yeast DNA polymerase I and yeast DNA polymerase II can be separated by DEAE-cellulose, hydroxylapatite, and denatured DNA-cellulose chromatography from the postmitochondrial supernatants of yeast lysates. The yeast polymerases are both of high molec...
متن کاملPhotoreactivation of Transforming DNA by an Enzyme from Bakers' Yeast
Ultraviolet-inactivated Hemophilus influenzae transforming DNA recovers its activity when mixed with cell-free extracts of bakers' yeast and exposed to visible light. The active agent in the extract is not used up in the reaction, and purification has not separated it into more than one non-dialyzable component. It differs from the agent in Escherichia coli extract, which produces very similar ...
متن کاملPolymerase and Exonuclease Activities in Herpes Simplex Virus Type 1 DNA Polymerase Are Not Highly Coordinated
The herpes polymerase-processivity factor complex consists of the catalytic UL30 subunit containing both polymerase and proofreading exonuclease activities and the UL42 subunit that acts as a processivity factor. Curiously, the highly active exonuclease has minimal impact on the accumulation of mismatches generated by the polymerase activity. We utilized a series of oligonucleotides of defined ...
متن کاملTHE CALCIUM BINDING SITES OF THE BAKERS' YEAST TRANSKETOLASE
The calcium binding sites of Bakers' Yeast Transketolase (TK) was elucidated by estimating the pKa values of the functional groups that bind to calcium. These pKa's were found to be 6.25 and 7.2 relating to the pKa's of the two immidazol moieties of histidine residues on the enzyme. The rate of the binding of calcium to the enzyme was obtained separately as a function of pH. Maximum values ...
متن کاملFormaldehyde dehydrogenase from bakers' yeast.
In the course of studies of formaldehyde metabolism in yeast (I), an enzyme was found that catalyzed the oxidation of formaldehyde in the presence of glutathione and diphosphopyridine nucleotide. A similar enzyme was discovered independently by Strittmatter and Ball in liver (2). This paper describes the partial purification and some of the properties of yeast formaldehyde dehydrogenase. Some e...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1973
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1973.tb02576.x