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Biomedical subjects

D H Williams

Publications and source records attributed to D H Williams.

At least 199 records · Page 11Linked to original sources
PubMed1971

Determination of the sequences of protein-derived peptides and peptide mixtures by mass spectrometry.

Micro-quantities of protein-derived peptides have been converted into N-acetylated permethyl derivatives, and their sequences determined by low-resolution mass spectrometry without prior knowledge of their amino acid compositions or lengths. A new strategy is suggested for the mass spectrometric sequencing of oligopeptides or proteins, involving gel filtration of protein hydrolysates and subsequent sequence analysis of peptide mixtures. Finally, results are given that demonstrate for the first time the use of mass spectrometry for the analysis of a protein-derived peptide mixture, again without prior knowledge of the protein or components within the mixture.

Amino Acid Sequence↗
PubMed1967

A taxonomy of continuing medical education endeavour.

Five basic forms of continuing educational endeavour by physicians are listed in rank order. These components constitute an indivisible unit bound together by self-learning. The scholarly habit of planned daily reading and study in a home library-sanctuary as an integral part of a physician's workday heads the list. Day-to-day informal and formal colleague-association in patient care in the community and teaching hospital, in group practice and by consultation is the present major form of continuing educational endeavour. Emphasized is the sabbatical return every three to five years for three months at least to the teaching hospital to reinforce scholarly motivation and attitudes and to acquire new skills and knowledge. Attendance at scientific sessions of learned professional societies and short courses should be accompanied by presession and post-session guided reading to be undertaken in the physician's home library-sanctuary.

Adult↗
PubMed1966

Thermostability of Bacillus cereus penicillinase.

Williams, Daniel H., III (Hahnemann Medical College, Philadelphia, Pa.), A. Bondi, A. G. Moat, and F. Ahmad. Thermostability of Bacillus cereus penicillinase. J. Bacteriol. 91:257-261. 1966.-The extracellular penicillinase of Bacillus cereus, strain 13-10, exhibited an unusual thermostability. Whereas it was completely and irreversibly inactivated by heating at 70 C, it retained considerable activity when heated at 100 C for 30 min. The active enzyme remaining was completely stable to further heating at temperatures from 40 to 100 C for as long as 1 hr. Preparations of the enzyme heated to 100 C possessed pH (7.0) and temperature (37 C) optima identical with the unheated enzyme. Furthermore, both enzyme preparations exhibited identical combining capacity for the substrate (penicillin G), suggesting that the two preparations had similar hydrolytic properties. Our findings suggest that heating of penicillinase at 100 C results in the formation of a protein complex which is resistant to further denaturation by heat and other agents. Addition of certain metal ions to the enzyme solution before heat treatment increased the stability to heat at 100 C by virtue of their ability to induce complex formation. Pectin was shown to decrease thermostability, presumably by preventing aggregation of proteins present in the enzyme preparations. The well-known stabilizing effect of gelatin may be attributed to its role in enhancing complex formation.

Bacillus cereus↗