A DNA-binding protein in the serum of certain mammalian species.
نویسندگان
چکیده
Various mammalian species contain an anionic serum protein that reacts specifically with native DNA. It is considerably less reactive with single-strand DNA and does not react with monodeoxyribonucleotides, homopolyribonucleotides, or duplexes of homopolyribonucleotides. Synthetic dA.dT was an effective inhibitor of the reaction with native DNA, while Micrococcus luteus DNA and dG.dC were not inhibitory. This protein was encountered in the course of studies on DNA antibodies. Although it reacted with red cells coated with DNA and gave agar precipitation bands, it was clearly distinct from DNA antibodies. It was found in the serum of all animals of a given species, migrated as an alpha-beta globulin, and did not crossreact with gammaglobulins. It reacted with DNA in solution to give precipitation curves that were strongly influenced by changes in ionic strength. The protein was isolated from canine serum by precipitation with DNA and purified to homogeneity, as judged by immunochemical and electrophoretic criteria.A similar protein was found in mink, equine, and other sera, but not in human sera. Previous studies on DNA antibodies in certain experimental animals may have given false positive results due to this protein.
منابع مشابه
In silico investigation of lactoferrin protein characterizations for the prediction of anti-microbial properties
Lactoferrin (Lf) is an iron-binding multi-functional glycoprotein which has numerous physiological functions such as iron transportation, anti-microbial activity and immune response. In this study, different in silico approaches were exploited to investigate Lf protein properties in a number of mammalian species. Results showed that the iron-binding site, DNA and RNA-binding sites, signal pepti...
متن کاملINVESTIGATIONS ON THE DRUG-PROTEIN IN TERAC TION OF CERTAIN NEW POTENTIAL LOCAL ANAESTHETICS
Generally, plasma proteins owe their binding capacity to the presence of aminoacid units which enter into intra- and intermolecular hydrophobic bonding with a diverse range of endo- and exogenous chemical substances. The intermolecular interactions between the hydrophobic areas of drug molecules and those of plasma proteins play an important role in drug-macromolecular complex formation and...
متن کاملRapid purification of HU protein from Halobacillus karajensis
The histone-like protein HU is the most-abundant DNA-binding protein in bacteria. The HU protein non-specifically binds and bends DNA as a hetero- or homodimer, and can participate in DNA supercoiling and DNA condensation. It also takes part in DNA functions such as replication, recombination, and repair. HU does not recognize any specific sequences but shows a certain degree of specificity to ...
متن کاملSPECTROSCOPIC EVALUATION OF THE INTERACTION OF A TETRAZOLE DERIVATIVE SYNTHESIZED BY SEMI-GREEN METHOD WITH CALF THYMUS DNA AND BOVINE SERUM PROTEIN
Background & Aims: In recent decades, the application of tetrazole structures in various fields of medicine and industry has become very important, because they can cause structural and thus functional changes in the proteins. In this article, the effect of a new tetrazole derivative on calf thymus DNA (Ct-DNA) as well as on bovine serum albumin protein (BSA) in the solution was determined usin...
متن کاملEvolutionary Analysis of Mammalian ACE2 and the Key Residues Involved in Binding to the Spike Protein Revealed Potential SARS-CoV-2 Hosts
Introduction: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spilled over to humans via wild mammals, entering the host cell using angiotensin-converting enzyme 2 (ACE2) as receptor through Spike (S) protein binding. While SARS-CoV-2 became fully adapted to humans and globally spread, some mammal species were infected back. The present study evaluated the potential risk of mammals...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 69 11 شماره
صفحات -
تاریخ انتشار 1972