{"title":"Synthesis and properties of N-, O-, and S-phospho derivatives of amino acids, peptides, and proteins.","authors":"A W Frank","doi":"10.3109/10409238409102806","DOIUrl":"https://doi.org/10.3109/10409238409102806","url":null,"abstract":"<p><p>The literature on chemical (i.e., nonenzymic) phosphorylation of amino acids, peptides, and proteins is reviewed through 1982. The review covers synthetic methods, chemical reactions, and physical properties, with emphasis on the techniques used for separation and characterization of the products. Synthetic methods are classified by reagent rather than product, and are illustrated by experimental procedures for the most important methods. Chemical reactions are classified into four groups depending on whether the reaction site is the phospho group, the amino group, the carboxyl group, or in the case of serine the hydroxyl group. Physical data are given for all of the known N-, O-, and S-phospho derivatives of the amino acids, peptides, and proteins, within certain limitations, and are discussed in detail in the section on physical properties. Emphasis is given to the techniques used for separation of the products, such as chromatography and electrophoresis, and for characterization of the products, particularly spectroscopy. Medical and other uses of the products are mentioned.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"16 1","pages":"51-101"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409102806","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17385840","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Thermodynamics of hapten-antibody interactions.","authors":"T K Mukkur","doi":"10.3109/10409238409102301","DOIUrl":"https://doi.org/10.3109/10409238409102301","url":null,"abstract":"<p><p>Two schools of thought are currently prevalent regarding the thermodynamic mechanism(s) of hapten-antibody interaction(s). While one school is a proponent of the hapten-antibody reaction being driven predominantly by enthalpy, the second school rationalizes the mechanism as an enthalpy-entropy compensation, the magnitude of the latter being dependent on the temperature at which hapten-antibody interaction is carried out.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"16 2","pages":"133-67"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409102301","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17435895","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Dye-ligand affinity chromatography: the interaction of Cibacron Blue F3GA with proteins and enzymes.","authors":"S Subramanian","doi":"10.3109/10409238409102302","DOIUrl":"https://doi.org/10.3109/10409238409102302","url":null,"abstract":"<p><p>The dye Cibacron Blue F3GA has a high affinity for many proteins and enzymes. It has therefore been attached to various solid supports such as Sephadex, Sepharose, polyacrylamide, and the like. In the immobilized form the dye has rapidly been exploited as an affinity chromatographic medium to separate and purify a variety of proteins including dehydrogenases, kinases, serum albumin, interferons, several plasma proteins, and a host of other proteins. Such a diversity shown by the blue dye in binding several unrelated classes of proteins has generated considerable work in terms of studies of the chromophore itself and also the immobilized ligand. As a prelude to realizing the full potential of the immobilized Cibacron Blue F3GA, an understanding of the basic interactions of the dye with its surroundings must be gained. It has been recognized that the dye is capable of hydrophobic and/or electrostatic interactions at the instance of the ambient conditions. The study of interactions of the dye with salts, solvents, and other small molecules indicates the nature of the interactions of the dye with different kinds of groups at the interacting sites of proteins. The review will cover such interactions of the dye with the proteins, the interactions of the proteins with the immobilized ligand, and the media used to elute the bound protein in several cases, and thus consolidate the available information on such studies into a cogent and comprehensive explanation.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"16 2","pages":"169-205"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409102302","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17267883","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Introduction of purified genes into mammalian cells.","authors":"R Kucherlapati, A I Skoultchi","doi":"10.3109/10409238409108719","DOIUrl":"https://doi.org/10.3109/10409238409108719","url":null,"abstract":"<p><p>There are a number of methods to introduce genes into mammalian cells. These include cell hybridization, chromosome-mediated and DNA-mediated gene transfer. DNA-mediated transfer can be achieved by direct microinjection methods or by indirect methods. The DNA enters the nucleus and is expressed in a high proportion of cells transiently. The DNA then becomes integrated into host cell DNA at random sites resulting in more stably expressing transformants. A number of genes for which selection systems exist can be introduced into mammalian cells. Nonselectable genes can also be introduced into cells by either ligating them to a selectable gene or by mixing them with carrier DNA and a selectable gene. If an amplifiable gene sequence is introduced into cells, it and other genes in its proximity can be coamplified. Amplification of the genes can also be achieved by the use of appropriate viral vectors and recipient cells. The foreign genes are expressed in the recipient cells if they contain the appropriate recognition signals for initiation and termination of transcription. Transfection systems are thus permitting identification of DNA sequences which have a regulatory role in gene expression. The identification of transcriptional signal sequences has formed the basis for construction of appropriate molecules which would permit expression of genes which cannot normally be expressed in mammalian cells (e.g., bacterial genes). The foreign genes are not only expressed in the recipient cells but they can also be subject to regulation in the appropriate environment. This observation is paving the way for identification of regulatory sequences. The foreign DNA sequences integrated into the host genome can be recovered by a variety of methods. Such methods permit isolation of genes which code for a selectable gene product.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"16 4","pages":"349-79"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409108719","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17161311","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Processing of tRNA in prokaryotes and eukaryotes.","authors":"M P Deutscher","doi":"10.3109/10409238409110269","DOIUrl":"https://doi.org/10.3109/10409238409110269","url":null,"abstract":"<p><p>Considerable progress has been made in defining the steps in the conversion of a tRNA precursor to a mature tRNA. These steps, which differ in different systems, include removal of precursor-specific residues from the 5' and 3' termini of the initial transcript, addition of the 3'-C-C-A terminus, splicing of intervening sequences, and modification of nucleotide residues. Despite these advances in defining the \"pathways\" of tRNA processing, relatively little is known about most of the enzymes actually involved in these processing steps. In this article I describe the sequence of reactions needed to convert the initial tRNA transcript to a functional, mature tRNA, and discuss the specificity and properties of enzymes known to be involved in this process. In addition, I speculate on the expected specificities of other enzymes involved in tRNA processing which have not yet been identified, and on the structural organization of the processing machinery.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"17 1","pages":"45-71"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409110269","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17161314","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The synthesis and biology of fluorinated prostacyclins.","authors":"W. E. Barnette","doi":"10.3109/10409238409102802","DOIUrl":"https://doi.org/10.3109/10409238409102802","url":null,"abstract":"Fluorination has been used extensively in the steroid field to alter and/or enhance activity and to increase chemical or biological stability taking advantage of the similarity in size between hydrogen and fluorine and its strong electronegativity. Thus, it is not surprising to find that the same principle has been applied to prostaglandins, more specifically prostacyclin. The specific activity and high instability of Prostacyclin make it an ideal candidate for similar fluorination techniques. The design and preparation of fluorinated analogs with the aim of improving the chemical and metabolic stability of this important molecule will be discussed.","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"94 1","pages":"201-35"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409102802","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69419416","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Structural and functional aspects of domain motions in proteins.","authors":"W S Bennett, R Huber","doi":"10.3109/10409238409117796","DOIUrl":"https://doi.org/10.3109/10409238409117796","url":null,"abstract":"<p><p>Three distinct categories of large-scale flexibility in proteins have been documented by single-crystal X-ray diffraction studies: the relatively free movement of essentially rigid globular domains that are connected by a flexible segment of polypeptide, the reorientation of essentially rigid domains among a few distinct conformations, and the concerted transition of a contiguous region of the surface of a protein from a disordered state to an ordered state. In a number of examples, well-defined functions can be assigned to these large-scale structural changes. The occurrence of such motions in proteins of known structure is reviewed, and the best-studied examples are discussed in detail to allow a critical evaluation of the methods used to identify and study these motions.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"15 4","pages":"291-384"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409117796","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17385839","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The proton inventory technique.","authors":"K S Venkatasubban, R L Schowen","doi":"10.3109/10409238409110268","DOIUrl":"https://doi.org/10.3109/10409238409110268","url":null,"abstract":"<p><p>The proton inventory technique uses the dependence of enzymic reaction rate on the atom fraction of deuterium present in mixtures of protium oxide and deuterium oxide to deduce for simple cases the number of exchangeable hydrogenic sites that produce isotope effects, and the magnitude of the isotope effect generated at each site. For more complex cases, other information, such as the participation of more than a single step in limiting the rate, may be obtained. The background of the method, the conduct of the experiments and the interpretation of the results are briefly reviewed. The method is then illustrated in its application to various enzyme systems by a series of case histories.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"17 1","pages":"1-44"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409110268","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17161313","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Sucrase-isomaltase: a stalked intrinsic protein of the brush border membrane.","authors":"H Hauser, G Semenza","doi":"10.3109/10409238309102798","DOIUrl":"https://doi.org/10.3109/10409238309102798","url":null,"abstract":"<p><p>The isolation and purification of sucrase-isomaltase from brush border membrane is described and the physicochemical properties of the pure enzyme are discussed. Our present understanding of the mode of association of the intrinsic membrane protein sucrase-isomaltase with the brush border membrane will be the central point of this contribution. The assembly of sucrase-isomaltase into phospholipid bilayers has been reported to result in a model membrane system which resembles the \"native\" brush border membrane as regards the mode of lipid-protein interaction. The physicochemical properties of this reconstituted model membrane will be compared to the in vivo situation as represented by brush border membrane vesicles routinely isolated from small intestinal brush borders. The biosynthetic mechanism will be discussed.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"14 4","pages":"319-45"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238309102798","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17418597","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Conformation and activity of beta-lactam antibiotics.","authors":"V S Rao, T K Vasudevan","doi":"10.3109/10409238309102793","DOIUrl":"https://doi.org/10.3109/10409238309102793","url":null,"abstract":"","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"14 3","pages":"173-206"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238309102793","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17414231","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}