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  Pediatric body MRI : a comprehensive, multidisciplinary guide

  edited by Edward Y. Lee, Mark C. Liszewski, Michael S. Gee, Pedro Daltro, Ricardo Restrepo.

  Summary: This book is a unique, authoritative and clinically oriented text on pediatric body MRI. It is your one-step reference for current information on pediatric body MRI addressing all aspects of congenital and acquired disorders. The easy-to-navigate text is divided into 17 chapters. Each chapter is organized to comprehensively cover the latest MRI techniques, fundamental embryology and anatomy, normal development and anatomic variants, key clinical presentation, characteristic imaging findings with MRI focus, differential diagnosis and pitfalls, as well as up-to-date management and treatment. Written by internationally known pediatric radiology experts and editorial team lead by acclaimed author, Edward Y. Lee, MD, MPH, this book is an ideal guide for practicing radiologists, radiology trainees, MRI technologists as well as clinicians in other specialties who are interested in pediatric body MRI.
  
  Contents:
  SECTION I: MRI of Pediatric Thorax
  Lung and Pleura
  Large Airways
  Great Vessels
  Mediastinum
  Chest Wall and Diaphragm
  SECTION II: MRI of Pediatric Abdomen and Pelvis
  Liver
  Bile Duct and Gallbladder
  Pancreas
  Spleen
  Adrenal Glands
  Gastrointestinal Tract
  Kidney, Ureter, and Bladder
  Male Genital Tract
  Female Genital Tract
  Peritoneum and Retroperitoneum.

  Digital Access Springer 2020
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• Article

  The synthesis of cytochrome b on mitochondrial ribosomes in baker's yeast.

  Lin LF, Clejan L, Beattie DS.

  Eur J Biochem. 1978 Jun 01;87(1):171-9.

  Antiserum against a major cytochrome b peptide isolated from yeast mitochondria as described previously (Lin, L.-F.H., and Beattie, D.S., J. Biol. Chem. 1978, 253, 2412--2418) was raised in rabbits and shown to be monospecific against the pure antigen. Mitochondria were isolated from yeast cells grown in [3H]leucine, extracted with Lubrol and treated with antiserum to cytochrome b. Analysis of the immunoprecipitates by sodium dodecyl sulfate/polyacrylamide gel electrophoresis revealed the presence of a single major band of molecular weight 31 000 corresponding to cytochrome b. In order to determine the intracellular site of translation of cytochrome b, yeast cells were labeled in vivo under non-growing conditions with [3H]leucine in the absence or presence of inhibitors of cytoplasmic and mitochondrial protein synthesis. The incorporation of radioactive leucine into the apoprotein of cytochrome b isolated by immunoprecipitation followed by gel electrophoresis was insensitive to cycloheximide (an inhibitor of cytoplasmic protein synthesis) and sensitive to acriflavin, erythromycin, and chloramphenicol (inhibitors of mitochondrial protein synthesis). Furthermore, no cytochrome b apoprotein was present in a cytoplasmic petite mutant which lacked mitochondrial protein synthesis. Cytochrome b is thus a product of protein synthesis on mitochondrial ribosomes.

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  PubMed