Pennsylvania Mining Families: The Search for Dignity in the Coalfields

In Pennsylvania Mining Families, Barry P. Michrina offers a luminous portrait of Pennsylvania coal miners and their response to economic oppression. He follows them from the great coal strike of 1927 through daily threats of injury and death in the mines to the departure of children and grandchildren as the industry has declined. Drawing on numerous first-hand interviews, as well as extensive archival research, he analyzes the change in work practices, the miners’ own views about their ever-evolving situation, and relationships between miners and mining companies—undercutting the stereotypical picture of the rebellious miner. Barry P. Michrina, professor of anthropology at Colorado Mesa University, is the author of Person to Person: Fieldwork, Dialogue, and the Hermeneutic Method. An in-depth look at the day-to-day events that faced working men and their families in the central Pennsylvania coal region from the 1920s to the 1950s. . . . [The stories] are told in the words of people who lived the events and are supported with empirical evidence -- Pennsylvania Geographer Michrina brings to his unusual and universal \u27true\u27 tales the sensitivity, style, and ironic distance of a great fiction writer. A wonderful book. -- Booklist Should be on the reading list of every scholar or student who wants to understand the fieldwork process more fully -- Journal of American Folklorehttps://uknowledge.uky.edu/upk_labor_history/1000/thumbnail.jp

Dictyostelium discoideum salvages purine deoxyribonucleosides by highly specific bacterial-like deoxyribonucleoside kinases

The salvage of deoxyribonucleosides in the social amoeba Dictyostelium discoideum, which has an extremely A + T-rich genome, was investigated. All native deoxyribonucleosides were phosphorylated by D. discoideum cell extracts and we subcloned three deoxyribonucleoside kinase (dNK) encoding genes. D. discoideum thymidine kinase was similar to the human thymidine kinase 1 and was specific for thymidine with a k(m) of 5.1 mu M. The other two cloned kinases were phylogenetically closer to bacterial deoxyribonucleoside kinases than to the eukaryotic enzymes. D. discoideum deoxyadenosine kinase (DddAK) had a K-m for deoxyadenosine of 22.7 mu M and a k(cat) of 3.7 s(-1) and could not efficiently phosphorylate any other native deoxyribonucleoside. D. discoideum deoxyguanosine kinase was also a purine-specific kinase and phosphorylated significantly only deoxyguanosine, with a K-m of 1.4 mu M and a k(cat) of 3 s(-1). The two purine-specific deoxyribonucleoside kinases could represent ancient enzymes present in the common ancestor of bacteria and eukaryotes but remaining only in a few eukaryote lineages. The narrow substrate specificity of the D. discoideum dNKs reflects the biased genome composition and we attempted to explain the strict preference of DddAK for deoxyadenosine by modeling the active center with different substrates. Apart from its native substrate, deoxyadenosine, DddAK efficiently phosphorylated fludarabine. Hence, DddAK could be used in the enzymatic production of fludarabine monophosphate, a drug used in the treatment of chronic lymphocytic leukemia