Dr. PrahlHe was an associate professor in the pathology department at the University of Utah School of Medicine where he was teaching and doing research on the complement system. A member of the National Institutes of Health Allergy and Immunology Study Section and the American Heart Association Immunology and Microbiology Research Study Committee, he also was an associate editor of the Journal of Immunology, an advisory editor of Immunochemistry {Molecular Immunology), and on the editorial board of Archives of Biochemistry.Biophysics. He was a member of several professional organizations including the American Association of Immunologists, the American Society of Biological Chemists, and the British Biochemical Society.

Dr. Prahl was born in New York City in 1931. He graduated from Princeton University cum laude in 1953 and received his MD in 1957 from the University of Pennsylvania School of Medicine. Between an internship and residency in internal medicine at Virginia Mason Hospital in Seattle, he served two years as a Senior Assistant Surgeon in the Public Health Service, Indian Health Service, New Mexico. Later, he enrolled as a doctoral candidate in the Department of Biochemistry of the University of Washington School of Medicine. He received his PhD in 1964 under Hans Neurath and subsequently did postdoctoral research on the structure of immunoglobulins in the laboratory of Rodney Porter, St. Mary's Hospital Medical School, and on complement in the laboratory of Hans Miiller-Eberhard at Scripps Clinic and Research Foundation. After working at the California Institute of Technology, he headed the Immunochemistry Section of the American Red Cross Blood Research Laboratory. During the following three years he organized a group active in the isolation and chemical characterization of several human complement proteins. He joined the faculty at the University of Utah in 1975.

Significant Contributions

Dr. Prahl made significant contributions to the field of immunology in two major areas. He studied the structure of immunoglobulins focusing on human heavy chains and their variants and the structural correlates of the allotypes in the rabbit. He later became interested in the complement system, and developed procedures for the isolation of large quantities of highly pure C3, C4, and C5. He elucidated many structural characteristics of these components, both native and activated, and was ultimately interested in relating structure to function. He had also begun studies into the mechanism of the binding of C3 and C4 to membranes, the structural basis of the genetic polymorphism of C3, and the biosynthesis of C4.


Colleagues who had the opportunity to work alongside Dr. Prahl in the laboratory admired his energy and the extraordinary intellectual capacities he brought to his fields of interest. He was creative about his work, applying novel approaches to his research and questioning generally accepted theories. He was exacting in his work, and his enthusiasm for research inspired those around him to demand more from themselves. He allowed the people who worked with him room to grow and develop their own capabilities supporting their aspirations and delighting in their accomplishments.


Dr. Prahl approached life with joy and enthusiasm. He loved his work, but also made time for traveling, mountain-climbing, skiing, and cultural activities. He was bright and energetic as well as kind and generous. He cared about people and those around him tended to reciprocate. He has been deeply missed.

Selected Publications

  • Evidence for presence of an internal thioester bond in third component of human complement. Tack BF, Harrison RA, Janatova J, Thomas ML, Prahl JW. Proc Natl Acad Sci U S A. 1980 Oct;77(10):5764-8. PMID: 6934510
  • Third component of human complement: structural requirements for its function. Janatova J, Tack BF, Prahl JW. Biochemistry. 1980 Sep 16;19(19):4479-85. PMID: 7407086
  • Third component of human complement: appearance of a sulfhydryl group following chemical or enzymatic inactivation. Janatova J, Lorenz PE, Schechter AN, Prahl JW, Tack BF. Biochemistry. 1980 Sep 16;19(19):4471-8. PMID: 7407085
  • Third component of human complement: structural analysis of the polypeptide chains of C3 and C3b. Tack BF, Morris SC, Prahl JW. Biochemistry. 1979 Apr 17;18(8):1497-503. PMID: 427127
  • Fifth component of human complement: purification from plasma and polypeptide chain structure. Tack BF, Morris SC, Prahl JW. Biochemistry. 1979 Apr 17;18(8):1490-7. PMID: 106884
  • Third component of human complement: purification from plasma and physicochemical characterization. Tack BD, Prahl JW. Biochemistry. 1976 Oct 5;15(20):4513-21. PMID: 823964
  • The complement system: a progress report. Prahl JW. Prog Clin Biol Res. 1976;5:43-67. PMID: 972914
  • Chemical studies of the heavy chain of rabbit IgG lacking group a allotypic markers. Prahl JW, Tack BF, Todd CW. Ann Immunol (Paris). 1974 Jan;125C(1-2):99-106. PMID: 4142573
  • Rabbit immunoglobulin lacking group a allotypic specificities. I. Isolation and nature of heavy chain. Tack BF, Feintuch K, Todd CW, Prahl JW. Biochemistry. 1973 Dec 4;12(25):5172-7. PMID: 4802020
  • Rabbit immunoglobulin lacking group a allotypic specificities. 3. Variable region structure and genetic control. Prahl JW, Tack BF, Todd CW. Biochemistry. 1973 Dec 4;12(25):5181-6. PMID: 4792302
  • Rabbit immunoglobulin lacking group a allotypic specificites. II. Retention of constant region d-11 and d-12 specificities. Tack BF, Prahl JW, Todd CW. Biochemistry. 1973 Dec 4;12(25):5178-80. PMID: 4792301
  • Restricted structural heterogeneity in antibodies: might different heavy chains have a common light chain? Waterfield MD, Prahl JW, Hood LE, Kindt TJ, Krause RM. Nat New Biol. 1972 Dec 13;240(102):215-7. PMID: 4509142
  • Genetic control of rabbit H chain biosynthesis. Prahl JW, Todd CW. Ann N Y Acad Sci. 1971 Dec 31;190:161-9. PMID: 5290011
  • Carboxy-terminal structure of the chain of human IgA myeloma proteins. Prahl JW, Abel CA, Grey HM. Biochemistry. 1971 May 11;10(10):1808-12. PMID: 4998234
  • Structural studies of human gamma D myeloma protein. Spiegelberg HL, Prahl JW, Grey HM. Biochemistry. 1970 May 12;9(10):2115-22. PMID: 4245598
  • The molecular determinants of the A11 and A12 allotypic specificities in rabbit immunoglobulin. Prahl JW, Mandy WJ, Todd CW. Biochemistry. 1969 Dec;8(12):4935-40. PMID: 4983541
  • Allotype-related sequence variation of the heavy chain of rabbit immunoglobulin G. Prahl JW, Porter RR. Biochem J. 1968 May;107(6):753-63. PMID: 16742601
  • The C-terminal sequences of the heavy chains of human immunoglobulin G myeloma proteins of differing isotopes and allotypes. Prahl JW. Biochem J. 1967 Dec;105(3):1019-28. PMID: 16742526
  • N- and C-terminal sequences of a heavy chain disease protein and its genetic implications. Prahl JW. Nature. 1967 Sep 23;215(5108):1386-7. PMID: 4168059
  • Enzymic degradation of the Fc fragment of rabbit immunoglobulin IgG. Prahl JW. Biochem J. 1967 Aug;104(2):647-55. PMID: 4167413
  • Pancreatic enzymes of the spiny Pacific dogfish. I. Cationic chymotrypsinogen and chymotrypsin. Prahl JW, Neurath H. Biochemistry. 1966 Jun;5(6):2131-46. PMID: 5963456
  • Metabolism of lactate in alloxan diabetic acidosis. Steenrod WJ Jr, Prahl JW, Barron EJ. Diabetes. 1966 Jun;15(6):423-9. PMID: 4957017
  • PRODUCTION OF ALLOXAN DIABETES AND KETOACIDOSIS IN THE LABORATORY RAT. PRAHL JW, STEENROD WJ Jr. Diabetes. 1965 May;14:289-94. PMID: 14280370