A 'what if' scenario for telemedicine reimbursement based on ATSP/TT survey findings.
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Biomedical subjects
Publications and source records attributed to F Fields.
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Existing breast self-examination (BSE) educational approaches have not been successful in gaining older women's compliance in proficient BSE. The experimental study detailed in this article was designed to determine whether there is a difference in BSE performance between women taught BSE individually using self-modeling in addition to a breast model (experimental group) and women taught BSE in a group using only a breast model (control group). Seventy-nine women, age 50 and older, randomly were assigned to the experimental and the control group. A pretest, a post-test immediately after the instruction, and a second post-test three months later involved BSE specialists observing each woman performing examinations on her own breast and on a breast model. A paired comparisons study yielded a set of weights that was used in calculating performance scores. Repeated measures analysis indicated that women in the experimental group performed BSE significantly more proficiently than women in the control group (F = 3.27, df = 2, 140, p = 0.041).
A human alpha interferon, designated HuIFN-alpha A, produced in E. coli by direct expression of cloned cDNA [Goeddel et al., Nature 287, 411--416 (1980)] has been purified from bacterial extracts and characterized. The protein has a molecular weight (19,400 by SDS/PAGE) and amino acid composition consistent with the DNA sequence. The pI was determined to be 6.1. The molecule has a specific activity of 1.5 x 10(8) NIH reference units/mg of protein. The sequence of the first 35 amino acids is identical to that expected from the nucleotide sequence. About 50% of the molecules begin with the expected cysteine, and 50% begin with the initiator methionine which E. coli apparently did not remove efficiently. Analysis of a trypsin digest of the native molecule showed that all four of the molecule's cysteines are involved in disulfide bonds: Cys1 is bonded to Cys98, and Cys29 is bonded to Cys 138.