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Biomedical subjects

J Fink

Publications and source records attributed to J Fink.

At least 73 records · Page 4Linked to original sources
PubMed1993

IgE reactivity to 14-kD and 27-kD natural rubber proteins in latex-allergic children with spina bifida and other congenital anomalies.

We examined by immunoblotting sera from 39 latex-allergic patients, 19 from USA and 20 from Finland, including 15 children with spina bifida and 5 children with other congenital anomalies, for IgE antibodies to natural rubber latex (latex) antigens. IgE antibodies in 10 of the 12 (83%) US spina bifida patients and in 2 of the 3 Finnish spina bifida patients recognized a previously undescribed 27-kD antigen which, together with a 14- and a 20-kD peptide, appeared to be a major latex allergen. Two patients with other congenital anomalies, one from the US and one from Finland, also demonstrated anti-27-kD bands. IgE antibodies to the 27-kD antigen were not detected in other latex-allergic patients from the US or Finland although most of them showed IgE binding to 14- and/or 20-kD latex antigens. All 21 controls, including 3 spina bifida patients with no evidence of latex allergy, gave negative immunoblot results. This observation suggests that patients with spina bifida or other congenital anomalies who have been subject to multiple operations and other invasive therapeutic procedures may have been exposed to different antigenic source materials than other latex-allergic patients.

Adolescent↗
PubMed1989

The chemical synthesis of cecropin D and an analog with enhanced antibacterial activity.

Cecropin D was synthesized by solid-phase methods and shown to be homogeneous and of correct composition and molecular weight. It was indistinguishable from natural cecropin D and constitutes a structure proof for this peptide. Several analogs of cecropin D were synthesized and used to draw conclusions about the structural features contributing to antibacterial activity. They included [Lys1]cecropin D, [Gln3, Leu4] cecropin D, and cecropin D-(9-37). It was concluded that a strongly basic NH2-terminal segment is a prerequisite for antibacterial activity. A hybrid analog cecropin A-(1-11) D-(12-37) was designed and predicted to have enhanced potency. It was found to be 5 to 55 times as active as cecropin D against six of the bacteria tested and was slightly more active than cecropin A. However, against Bacillus subtilis Bs11 the analog was 6 times more active than cecropin A.

Amino Acid Sequence↗