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  • Book
    Bertalan Dudás.
    Summary: Visually engaging and easy to use, Human Histology: A Text and Atlas for Physicians and Scientists covers the normal histology of every organ in the human body. This book presents full-page high-definition photomicrographs for organs and tissues, followed by a compact and simple-to-read description of the structures identified on the micrographs, offering a clear, visual understanding of this complex subject. With over 300 outstanding images, this reference is an invaluable resource for every clinical researcher and pathologist in need of easily accessible, relatively simple but detailed enough information on normal histology of different organs systems. Due to its compact, but detailed layout, the volume is an excellent tool for medical board review and can be recommended for medical students and histology course directors.

    Contents:
    Basic Tissues
    Lymphatic System
    Cardiovascular System
    Integumentary System
    Digestive System I: Upper Alimentary Tract
    Digestive System II: Lower Alimentary Tract
    Digestive System III: Liver and Pancreas
    Respiratory System
    Urinary System
    Male Reproductive System
    Female Reproductive System
    Endocrine System
    Nervous System
    Sensory Organs.
    Digital Access ClinicalKey 2023
  • Article
    Scopes RK.
    Eur J Biochem. 1978 Nov 02;91(1):119-29.
    1. The binding of all four substrates to yeast phosphoglycerate kinase has been studied using a gel filtration technique. The binding of phosphate and sulphate anions has also been investigated. 2. Two sites for each adenine nucleotide were found, one site being weaker than the other by between 30 and 50-fold. Only one binding site for the phosphoglycerate substrates was found. 3. 1,3-Bisphosphoglycerate (1,3-P2-glycerate) bound to the enzyme approximately 1000 times tighter than the other three substrates, its dissociation constant being 0.06 micrometer at ionic strength 0.15 M. 4. Sulphate and phosphate were mutually competitive and sulphate competed with the binding of all substrates except MgADP. MgADP bound to the enzyme more weakly in the presence of sulphate. The dissociation constant for sulphate binding was 1.6 mM at ionic strength of 0.15 M, and 0.05 mM at ionic strength 0.015 M. 5. These results are consistent with sulphate acting as a competitive inhibitor, as found by kinetic studies at high sulphate concentrations. The activatory effect of sulphate at lower concentrations and the substrate activation phenomea displayed by this enzyme, are interpreted in terms of a two-step dissociation of 1, 3-P2-glycerate. The presence of moderate concentrations of MgATP, 3-phosphoglycerate or sulphate causes acceleration of the rate of dissociation of the product, 1, 3-P2-glycerate, this being the rate-limiting step in the overall enzyme reaction.
    Digital Access Access Options