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  • Book
    Kimberly C. Harper.
    Summary: This book discusses existing problems with Black maternal health and the rhetorical implications of ethos in American society. The Ethos of Black Motherhood in America: Only White Women Get Pregnant examines the ethos of Black and white mothers in America's racialized society. Kimberly C. Harper argues that the current Black maternal health crisis is not a new one, but an existing one rooted in the disregard for Black wombs dating back to America's history with chattel slavery. Examining the reproductive laws that controlled the reproductive experiences of black women, Harper provides a fresh insight into the “bad black mother” trope that Black feminist scholars have theorized and argues that the controlling images of black motherhood are a creation of the American nation-state. In addition to a discussion of black motherhood, Harper also explores the image of white motherhood as the center of the landscape of motherhood. Scholars of communication, gender studies, women's studies, history, and race studies will find this book particularly useful.

    Contents:
    Historical representations of Black motherhood
    Setting the tone
    The legislative decisions governing Black wombs
    Ideology, ethos, and silence
    Where are all the Black mothers in pregnancy books?
    Reproductive justice and Black women's lives
    Black midwives and reclaiming choice
    The will to resist is a form of love
    Conclusions.
    Digital Access ProQuest Ebook Central [2021]
  • Article
    Vickers LP, Donovan JW, Schachman HK.
    J Biol Chem. 1978 Dec 10;253(23):8493-8.
    The thermal denaturation of aspartate transcarbamoylas of Escherichia coli was investigated by differential scanning calorimetry. Isolated regulatory and catalytic subunits were heat denatured at 55 and 80 degrees C, respectively. In contrast, the intact enzyme was denatured in two steps. A small endotherm near 73 degrees C was assoicated with denaturation of the regulatory subunits and the major endotherm at 82 degrees C with denaturation of the catalytic subunits. Thus regulatory subunits are stabilized against heat denaturation by more than 17 degrees C when incorporated in the enzyme. Similar conclusions were obtained from measurements of the enthalpy of heat denaturation. Regulatory subunits yielded a much lower value of the enthalpy of denaturation, 1.91 cal/g, than that found for the catalytic subunit, 3.94 cal/g, or typical globular proteins (4 to 6 cal/g). When the regulatory subunits were incorporated into aspartate transcarbamoylase their enthalpy of denaturation was increased 125% (to 4.3 cal/g). The enthalpy of the catalytic subunits in the intact enzyme was increased 38% (enthalpy of denaturation of 5.43 cal/g). Stabilization of the isolated catalytic subunit as well as the intact enzyme was achieved by the addition of the bisubstrate analog N-(phosphonacetyl)-L-aspartate. Similarly the allosteric effectors, CTP and ATP, stabilized the isolated regulatory subunits or those subunits within the intact enzyme. However, the addition of the bisubstrate analog caused a decrease in the enthalpy of denaturation of the regulatory subunits within the enzyme. These results are consistent with other studies of the ligand-promoted conformational changes in the native enzyme.
    Digital Access Access Options