{"title":"Physicochemical properties of oilseed proteins.","authors":"V Prakash, M S Rao","doi":"10.3109/10409238609083736","DOIUrl":"10.3109/10409238609083736","url":null,"abstract":"<p><p>This review attempts to consolidate the information on the physicochemical properties of proteins from groundnut, soybean, sesame seed, mustard seed, rapeseed, sunflower seed, cottonseed, and other oilseeds. It deals with the extraction and characterization of the oilseed proteins and describes the methods for isolation of the various protein fractions and determination of their physicochemical characteristics. Also discussed are the subunit composition of the oligomeric proteins, their hydrodynamic properties, and the effect of denaturants on these proteins. The similarity in the properties of the proteins from various oilseed materials is discussed. The review article aims to indicate the gaps in our knowledge about the physicochemical properties of oilseed proteins and suggests areas for future investigation.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"20 3","pages":"265-363"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238609083736","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14642049","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":"Genes for cytochrome P-450 and their regulation.","authors":"M Adesnik, M Atchison","doi":"10.3109/10409238609084657","DOIUrl":"https://doi.org/10.3109/10409238609084657","url":null,"abstract":"<p><p>The capacity of the liver microsomal mixed-function oxidase system to metabolize a wide variety of exogenous as well as endogenous compounds reflects the participation of multiple forms of the terminal oxidase, cytochrome P-450, which have different broad, but overlapping, substrate specificities. Several of these isozymes accumulate in the liver after exposure of animals to specific inducing agents. Recent studies employing recombinant DNA techniques to investigate the genetic and evolutionary relatedness of various cytochrome P-450 isozymes as well as the molecular basis for the induction phenomenon are described. The conclusions from these investigations are presented in the context of the substantial body of data obtained from the characterization of specific cytochrome P-450 isozymes and from studies on the induction of specific isozymes or enzymatic activities during development or after treatment of animals with various inducing agents.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"19 3","pages":"247-305"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238609084657","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14635631","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":"Molecular biology of parathyroid hormone.","authors":"B Kemper","doi":"10.3109/10409238609082545","DOIUrl":"https://doi.org/10.3109/10409238609082545","url":null,"abstract":"<p><p>The entire biosynthetic pathway of PTH has been elucidated from the determination of the chromosomal location to the eventual secretion of the hormone from the cell. The human gene is present on the short arm of chromosome 11, and restriction site polymorphisms near the gene have been detected. The PTH genes and cDNAs have been isolated and characterized in the bovine, human, and rat species. The gene contains two introns, which are in the same position in each species, and dissect the gene into 3 exons that code, respectively, for the 5' untranslated region, the signal peptide, and PTH plus the 3' untranslated region. The mRNAs are about twice as long as necessary to code for preProPTH and contain a 7-methylquanosine cap at the 5' terminus and polyadenylic acid at the 3' terminus. The 5' termini of the bovine and human mRNAs are heterogeneous at the 5' terminus, the basis of which is two TATA sequences in the 5' flanking regions of the gene. In contrast, the rat gene contains a single TATA sequence and the mRNA has a single 5' terminus. The initial translational product of the mRNA is preProPTH, and the pre-peptide of 25 amino acids is equivalent to signal peptides of other secreted and membrane proteins. The genes of the three species are very homologous in the region that codes for preProPTH. Substantial homology is also retained in the gene flanking regions, introns, and mRNA untranslated regions. Silent sites are also conserved more than would be expected, particularly between the human and bovine sequences. The bovine and human sequences are more closely related than the rat is to either the human or bovine. These studies of the basic molecular biology of PTH will provide the framework for future analysis of significant biological and medical questions. In vitro mutagenesis techniques should soon provide information about the elements of the gene involved in regulating transcription and about functional elements of the signal peptide. Eventually, signals involved in directing the ProPTH molecule to secretory granules as well as the biologically active regions of PTH, itself, will be examined by these methods. The molecular biological studies, combined with the development of dispersed cell cultures, provide the opportunity to study the effects of chronic changes in calcium on gene transcription and mRNA metabolism. The restriction site polymorphisms associated with the human PTH gene will allow a search for correlations between PTH gene structure and parathyroid disease.(ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"19 4","pages":"353-79"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238609082545","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14639781","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":"Histones and their modifications.","authors":"R S Wu, H T Panusz, C L Hatch, W M Bonner","doi":"10.3109/10409238609083735","DOIUrl":"https://doi.org/10.3109/10409238609083735","url":null,"abstract":"<p><p>Histones constitute the protein core around which DNA is coiled to form the basic structural unit of the chromosome known as the nucleosome. Because of the large amount of new histone needed during chromosome replication, the synthesis of histone and DNA is regulated in a complex manner. During RNA transcription and DNA replication, the basic nucleosomal structure as well as interactions between nucleosomes must be greatly altered to allow access to the appropriate enzymes and factors. The presence of extensive and varied post-translational modifications to the otherwise highly conserved histone primary sequences provides obvious opportunities for such structural alterations, but despite concentrated and sustained effort, causal connections between histone modifications and nucleosomal functions are not yet elucidated.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"20 2","pages":"201-63"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238609083735","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14642112","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":"Organization of extracellularly mineralized tissues: a comparative study of biological crystal growth.","authors":"S Weiner","doi":"10.3109/10409238609081998","DOIUrl":"https://doi.org/10.3109/10409238609081998","url":null,"abstract":"<p><p>Biological mineralization processes are extremely diverse and, to date, it is an act of faith rather than an established principle that organisms utilize common mechanisms for forming crystals. A systematic analysis of the structural organization, as far as possible at the molecular level, of five different extracellularly mineralized tissues is presented to demonstrate that at least these mineralization processes are all part of the same continuum. The degrees of control exercised over crystal nucleation and crystal growth modulation are the basic variables. The five tissues, extracellularly mineralizing algae, radial and granular foraminifera, mammalian bone, mammalian enamel, and mollusk shell nacre, probably span the entire spectrum. Their crystal shapes, sizes, and the relations between the mineral phase and the organic phase, are primarily used to assess probable degrees of control exercised over crystal nucleation and modulation. Three different types of nucleation processes can be recognized: nonspecific, stereochemical, and epitaxial. Modulation of crystal growth after nucleation is either absent, achieved by adsorption of macromolecules onto specific crystal faces, or occurs by the prepositioning of matrix surfaces which interrupt crystal growth. The tissues in which active control is exercised over crystal growth all contain similar types of acidic matrix macromolecules. Significantly, the framework matrix macromolecules are all quite different and hence probably perform some tissue-specific functions. The study shows that there is a common basis for understanding these mineralization processes which is reflected in the nature of the protein-crystal interactions which occur in each tissue.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"20 4","pages":"365-408"},"PeriodicalIF":0.0,"publicationDate":"1986-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238609081998","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14647337","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 heat shock response.","authors":"E A Craig","doi":"10.3109/10409238509085135","DOIUrl":"https://doi.org/10.3109/10409238509085135","url":null,"abstract":"<p><p>The response of cells to a heat shock or other stresses is the activation of a small number of genes which were previously inactive or transcribed at low levels. This response has been observed in a wide variety of bacterial, plant, and animal species. Evidence is accumulating that at least some of the proteins found in diverse species are similar, indicating a conservation of the response and the proteins in evolution. In a number of organisms a strong positive correlation has been found between the presence of heat shock proteins and ability of the organism to withstand thermal stress. This review attempts to assess the available data concerning the homology of proteins in different species, the localization of the proteins in cells, and the relationship between heat shock proteins and thermoresistance.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"18 3","pages":"239-80"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238509085135","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13558973","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":"Porin from bacterial and mitochondrial outer membranes.","authors":"R Benz","doi":"10.3109/10409238509082542","DOIUrl":"https://doi.org/10.3109/10409238509082542","url":null,"abstract":"<p><p>The outer membrane of gram-negative bacteria acts as a molecular filter with defined exclusion limit for hydrophilic substances. The exclusion limit is dependent on the type of bacteria and has for enteric bacteria like Escherichia coli and Salmonella typhimurium a value between 600 and 800 Daltons, whereas molecules with molecular weights up to 6000 can penetrate the outer membrane of Pseudomonas aeruginosa. The molecular sieving properties result from the presence of a class of major proteins called porins which form trimers of identical subunits in the outer membrane. The porin trimers most likely contain only one large but well-defined pore with a diameter between 1.2 and 2 nm. Mitochondria are presumably descendents of gram-negative bacteria. The outer membrane of mitochondria contains in agreement with this hypothesis large pores which are permeable for hydrophilic substances with molecular weights up to 6000. The mitochondrial porins are processed by the cell and have molecular weights around 30,000 Daltons. There exists some evidence that the pore is controlled by electric fields and metabolic processes.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"19 2","pages":"145-90"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238509082542","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13564468","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":"Attenuation may regulate gene expression in animal viruses and cells.","authors":"Y Aloni, N Hay","doi":"10.3109/10409238509086785","DOIUrl":"https://doi.org/10.3109/10409238509086785","url":null,"abstract":"<p><p>In eukaryotes, an abundant population of promoter-proximal RNA chains have been observed and studied, mainly in whole nuclear RNA, in denovirus type 2, and in SV40. On the basis of these results it has been suggested that a premature termination process resembling attenuation in prokaryotes occurs in eukaryotes. Moreover, these studies have shown that the adenosine analog 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB) enhances premature termination, but its mode of action is not understood. The determination of the nucleotide sequences of SV40 and other viruses and cellular genes provide means for elucidating the nucleotide sequences involved in the attenuation mechanism. A model has recently been described in which attenuation and mRNA modulation in a feedback control system quantitatively regulate SV40 gene expression. The suggested mechanism described in this model opens up approaches to the investigation of attenuation and mRNA modulation as a possible mechanism whereby eukaryotes may regulate transcription in a variety of different circumstances.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"18 4","pages":"327-83"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238509086785","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14130448","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":"Curved DNA.","authors":"E N Trifonov","doi":"10.3109/10409238509082540","DOIUrl":"https://doi.org/10.3109/10409238509082540","url":null,"abstract":"<p><p>A priori considerations and the concept of the sequence-dependent local curving of the DNA axis. Experimental evidence: electric dichroism (relaxation time measurements); anomalous electrophoretic mobility and gel-filtration of some restriction fragments of DNA; one-sided binding of the nucleosomal DNA to the mica surface. Theoretical predictions concerning the nucleotide sequences of the curved DNA. Discovery of the dinucleotide periodicity in the chromatin DNA. The sequence periodicity as a tool for mapping of the nucleosomes along the sequences. Preferential binding of the histone octamers to the curved pieces of DNA--sequence analysis predictions and comparison with experiments: Theoretical and experimental estimates of the tilt and roll angles for different combinations of the neighboring base-pairs. Inherent sequence-dependent curvature and apparent persistence length of DNA.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"19 2","pages":"89-106"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238509082540","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15020824","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}