{"title":"Etheno-substituted nucleotides and coenzymes: fluorescence and biological activity.","authors":"N J Leonard","doi":"10.3109/10409238409102299","DOIUrl":"https://doi.org/10.3109/10409238409102299","url":null,"abstract":"AbstractDefinition of the individual adenine binding sites of enzymes is important for many reasons. Rendering an adenine moiety fluorescent while retaining the biological activity of the molecule of which it is a component can provide useful binding information because of the fluorescence properties. The 1,N6-ethenoadenosine phosphates and, similarly, e-modified polynucleotides, RNA, and DNA have been synthesized, and their spectroscopic properties and interactions have been studied in depth. The use of e-substituted nucleotides has helped to clarify numerous enzyme reactions, including those of ATPase and energy transfer, ATP transphosphorylase, glyceraldehyde-3-phosphate dehydrogenase, phosphofructokinase, phosphorylase b, protein kinase, pyruvate kinase, ribonucleases, RNA ligase, and others. The binding of e-substituted nucleotides or polynucleotides to proteins has been determined for F- and G-actin, heavy meromyosin, tobacco mosaic virus protein, gene 32 protein of bacteriophage T4, and chloroplast...","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"15 2","pages":"125-99"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409102299","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17424740","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":"Mechanistic studies of cAMP-dependent protein kinase action.","authors":"H N Bramson, E T Kaiser, A S Mildvan","doi":"10.3109/10409238409102298","DOIUrl":"https://doi.org/10.3109/10409238409102298","url":null,"abstract":"<p><p>The details of the process by which protein kinase catalyzes phosphoryl group transfers are beginning to be understood. Early work that explored the primary specificity of cAMP-dependent protein kinase action enabled the synthesis of small peptide substrates for the enzyme. Enzyme-peptide interactions seem simpler to understand than protein-protein interactions, so peptide substrates have been used in most protein kinase studies. In most investigations the kinetics for the phosphorylation of small peptides have been interpreted as being consistent with mechanisms which do not invoke phospho-enzyme intermediates (see, for example, Bolen et al.). Protein kinase has been shown to bind two metal ions in the presence of a nucleotide. Using magnetic resonance techniques the binding of these ions has been utilized to elucidate the conformation of nucleotide and peptide substrates or inhibitors when bound in the enzymic active site. Also, two new peptides with the form Leu-Arg-Arg-Ala-Ser-Y-Gly, where Y was either Pro or (N-methyl)Leu, were synthesized and found not to be substrates, within the limits of detection, for protein kinase. The striking lack of affinity that protein kinase has for such peptides which are unlikely to form a beta 3-6 turn has not been reported before. Our results may indicate that this type of turn is a requirement for protein kinase catalyzed phosphorylation or that these peptides lack the ability to form a particular hydrogen bond with the enzyme. Magnetic resonance techniques have indicated that the distance between the phosphorous in the gamma-phosphoryl group of MgATP and the hydroxyl oxygen of serine in the peptide Leu-Arg-Arg-Ala-Ser-Leu-Gly is 5.3 +/- 0.7 A. This, together with certain kinetic evidence, suggests that the mechanism by which protein kinase catalyzes phosphoryl group transfer has considerable dissociative character. Chemical modifications, including one using a peptide-based affinity label, have identified two residues at or near the active site, lysine-72 and cysteine 199. While neither of these groups has been shown to be catalytically essential, similar studies may help to identify groups that are directly involved in the catalytic process. Finally, a spectrophotometric assay for cAMP-dependent protein kinase has been described. Using this assay the preliminary results of an in-depth study of the pH dependence of protein kinase catalyzed phosphoryl group transfer have been obtained. This study shall aid in the identification of active site residues and should contribute to the elucidation of the enzyme's catalytic mechanism.(ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"15 2","pages":"93-124"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409102298","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17424741","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":"Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction.","authors":"P C Leavis, J Gergely","doi":"10.3109/10409238409108717","DOIUrl":"https://doi.org/10.3109/10409238409108717","url":null,"abstract":"<p><p>Recent developments in the field of myofibrillar proteins will be reviewed. Consideration will be given to the proteins that participate in the contractile process itself as well as to those involved in Ca-dependent regulation of striated (skeletal and cardiac) and smooth muscle. The relation of protein structure to function will be emphasized and the relation of various physiologically and histochemically defined fiber types to the proteins found in them will be discussed.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"16 3","pages":"235-305"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409108717","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17443515","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":"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":"The stereochemistry of peptides containing alpha-aminoisobutyric acid.","authors":"B V Prasad, P Balaram","doi":"10.3109/10409238409108718","DOIUrl":"https://doi.org/10.3109/10409238409108718","url":null,"abstract":"<p><p>The introduction of alpha-aminoisobutyric acid (Aib) into peptides dramatically limits the range of accessible backbone conformations. The presence of two geminal methyl groups at C alpha sterically compels Aib residues to largely favor structures in the right- or left-handed 3(10)/alpha-helical regions (phi approximately +/- 60 +/- 20 degrees, psi approximately +/- 30 +/- 20 degrees) of the peptide conformational map. Aib residues occur extensively in microbial peptides which form transmembrane channels. This observation has stimulated considerable interest in the stereochemistry of Aib peptides. This review summarizes theoretical studies on the conformations of Aib residues and examines the available data on solid-state structures, derived from single crystal X-ray diffraction studies. Crystal structures of over three dozen Aib-containing peptides, ranging in length from 2 to 11 residues, have been reported so far which exemplify various types of beta-turns, consecutive beta-turns, and helical structures. Examples of nonhydrogen bonded and cyclic structures are also described. The crystallographic results compare well with structural studies in solution, establishing that Aib peptides can provide rigid structural models for the development of spectroscopic methods of peptide conformational analysis.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"16 4","pages":"307-48"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409108718","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17449226","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":"Inhibitors of the biosynthesis and processing of N-linked oligosaccharides.","authors":"A D Elbein","doi":"10.3109/10409238409102805","DOIUrl":"https://doi.org/10.3109/10409238409102805","url":null,"abstract":"<p><p>A number of glycoproteins have oligosaccharides linked to protein in a GlcNAc----asparagine bond. These oligosaccharides may be either of the complex, the high-mannose or the hybrid structure. Each type of oligosaccharides is initially biosynthesized via lipid-linked oligosaccharides to form a Glc3Man9GlcNAc2-pyrophosphoryl-dolichol and transfer of this oligosaccharide to protein. The oligosaccharide portion is then processed, first of all by removal of all three glucose residues to give a Man9GlcNAc2-protein. This structure may be the immediate precursor to the high-mannose structure or it may be further processed by the removal of a number of mannose residues. Initially four alpha 1,2-linked mannoses are removed to give a Man5 - GlcNAc2 -protein which is then lengthened by the addition of a GlcNAc residue. This new structure, the GlcNAc- Man5 - GlcNAc2 -protein, is the substrate for mannosidase II which removes the alpha 1,3- and alpha 1,6-linked mannoses . Then the other sugars, GlcNAc, galactose, and sialic acid, are added sequentially to give the complex types of glycoproteins. A number of inhibitors have been identified that interfere with glycoprotein biosynthesis, processing, or transport. Some of these inhibitors have been valuable tools to study the reaction pathways while others have been extremely useful for examining the role of carbohydrate in glycoprotein function. For example, tunicamycin and its analogs prevent protein glycosylation by inhibiting the first step in the lipid-linked pathway, i.e., the formation of Glc NAc-pyrophosphoryl-dolichol. These antibiotics have been widely used in a number of functional studies. Another antibiotic that inhibits the lipid-linked saccharide pathway is amphomycin, which blocks the formation of dolichyl-phosphoryl-mannose. In vitro, this antibiotic gives rise to a Man5GlcNAc2 -pyrophosphoryl-dolichol from GDP-[14C]mannose, indicating that the first five mannose residues come directly from GDP-mannose rather than from dolichyl-phosphoryl-mannose. Other antibodies that have been shown to act at the lipid-level are diumycin , tsushimycin , tridecaptin, and flavomycin. In addition to these types of compounds, a number of sugar analogs such as 2-deoxyglucose, fluoroglucose , glucosamine, etc. have been utilized in some interesting experiments. Several compounds have been shown to inhibit glycoprotein processing. One of these, the alkaloid swainsonine , inhibits mannosidase II that removes alpha-1,3 and alpha-1,6 mannose residues from the GlcNAc- Man5GlcNAc2 -peptide. Thus, in cultured cells or in enveloped viruses, swainsonine causes the formation of a hybrid structure.(ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"16 1","pages":"21-49"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238409102805","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17294816","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":"","DOIUrl":"","url":null,"abstract":"<p><p>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.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"15 3","pages":"201-35"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17429558","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}