Updated from their original publication in 2004, these cancer genetic counseling recommendations describe the medical, psychosocial, and ethical ramifications of counseling at-risk individuals through genetic cancer risk assessment with or without genetic testing. They were developed by members of the Practice Issues Subcommittee of the National Society of Genetic Counselors Familial Cancer Risk Counseling Special Interest Group. The information contained in this document is derived from extensive review of the current literature on cancer genetic risk assessment and counseling as well as the personal expertise of genetic counselors specializing in cancer genetics. The recommendations are intended to provide information about the process of genetic counseling and risk assessment for hereditary cancer disorders rather than specific information about individual syndromes. Essential components include the intake, cancer risk assessment, genetic testing for an inherited cancer syndrome, informed consent, disclosure of genetic test results, and psychosocial assessment. These recommendations should not be construed as dictating an exclusive course of management, nor does use of such recommendations guarantee a particular outcome. These recommendations do not displace a health care provider's professional judgment based on the clinical circumstances of a client.
These cancer genetic counseling recommendations describe the medical, psychosocial, and ethical ramifications of identifying at-risk individuals through cancer risk assessment with or without genetic testing. They were developed by members of the Practice Issues Subcommittee of the National Society of Genetic Counselors Cancer Genetic Counseling Special Interest Group. The information contained in this document is derived from extensive review of the current literature on cancer genetic risk assessment and counseling as well as the personal expertise of genetic counselors specializing in cancer genetics. The recommendations are intended to provide information about the process of genetic counseling and risk assessment for hereditary cancer disorders rather than specific information about individual syndromes. Key components include the intake (medical and family histories), psychosocial assessment (assessment of risk perception), cancer risk assessment (determination and communication of risk), molecular testing for hereditary cancer syndromes (regulations, informed consent, and counseling process), and follow-up considerations. These recommendations should not be construed as dictating an exclusive course of management, nor does use of such recommendations guarantee a particular outcome. These recommendations do not displace a health care provider's professional judgment based on the clinical circumstances of a client.
We have developed a simple and efficient transformation system for the agaric fungus, Coprinus cinereus. Protoplasts were prepared from asexual spores that harbor one or two mutations in the structural gene for tryptophan synthetase. The protoplasts can be stably transformed using the cloned Coprinus gene at a frequency of 1 in 10(4) viable protoplasts. A variety of molecular events accompanies the formation of stable transformants, including insertion of the transforming DNA at the homologous locus. The transforming DNA is stable through cell division, mating, fruiting body formation, and meiosis.
The renaturation of Escherichia coli K 12 tryptophanase after treatment with 8 M urea has been studied. It is shown that, during the renaturation process, an inactive as well as an active form of the protein can be obtained. The influence on the relative amounts of these two forms of factors such as temperature, the presence of the coenzyme, the protein concentration and the conditions for removal of urea has been investigated. The results obtained indicate that the inactive form is characterized by incorrect quaternary interactions occurring specifically between tryptophanase protomers. These findings are discussed in the general frame of the mechanism of protein folding, and are taken as an evidence for the existence of nucleation centers in the folding of tryptophanase.Since the observation by White [l] and Anfinsen and Haber [2] that ribonuclease can be renatured after its complete unfolding with urea and reduction of its disulfides, many proteins have been successfully renatured by controlled removal of the denaturing agent. In spite of the many experimental studies reported, no general effect of various parameters (temperature, pH, ionic strength, etc.) on the yield and kinetics of the renaturation process has been observed: each protein responds differently to a change of these parameters during refolding. Yet, one observation appears to be rather general : the yield of renatured molecules from this process decreases at high protein concentration.While setting up a renaturation procedure for Escherichia coli K12 tryptophanase, we observed that this oligomeric enzyme [3,4] follows the general behaviour mentioned above. Using this system, we undertook experiments aimed at understanding the mechanism by which the protein concentration affects the renaturation process. In this paper, we describe a procedure for renaturing tryptophanase from 8 M urea with a high yield, compare some kinetic and hydrodynamic properties of the native and renatured enzymes, and report experiments showing that the renaturation process can, under controlled conditions, Enzymes. Tryptophanase (EC 4.1.99
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