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Biomedical subjects

P Stenzel

Publications and source records attributed to P Stenzel.

33 records · Page 2Linked to original sources
PubMed1984

Severe and prolonged oral contraceptive jaundice.

Oral contraceptives frequently produce mild hepatocellular dysfunction, but only rarely cause jaundice. The syndrome of oral contraceptive jaundice is usually mild, with rapid resolution upon withdrawal of the drug. We describe a patient who had a severe illness with marked jaundice after one cycle of oral contraceptives. Her symptoms progressively worsened and serum bilirubin increased for almost 3 months after discontinuation of oral contraceptives. Full recovery ultimately occurred. Her severe and prolonged course demonstrates the wide spectrum of oral contraceptive jaundice.

Adult↗
PubMed1983

Pouch ileitis: report of a case with severe systemic manifestations.

A 28-year-old man with chronic ulcerative colitis had a proctocolectomy with creation of a continent ileostomy. Six months later, he developed a severe systemic illness characterized by malaise, 24-lb. weight loss, fever, night sweats, arthralgias, bloody diarrhea, and problems with ileostomy function. On endoscopy, the pouch showed erythema, edema, friability, and ulceration; on biopsy, there was severe mucosal disruption with ulceration into the submucosa. Features consistent with chronic ulcerative colitis were also present. Laboratory investigation ruled out other causes of the illness so that a diagnosis of pouch ileitis was made. The patient responded dramatically to a 10-day course of metronidazole and remains well 2 years later. In patients with continent ileostomy after proctocolectomy for chronic ulcerative colitis, inflammation of the pouch may be associated with a severe systemic illness. The pathogenesis is unclear, but may involve the interaction of colonic type bacterial flora with ileal mucosa in immunologically susceptible patients.

Adult↗
PubMed1982

An X-linked syndrome of diarrhea, polyendocrinopathy, and fatal infection in infancy.

We have studied a patient from a family in which 17 male infants died in the first years of life. The clinical characteristics of this disorder were established from information from eight patients. The features included diarrhea, diabetes mellitus, hemolytic anemia, eczematoid rashes, and exaggerated responses to viral illnesses, combined with pathologic evidence of autodestruction of endocrine glands, insulitis, and thyroiditis with thyroid autoantibodies in one patient. When tested, B-lymphocyte cell function, T cell numbers, polymorphonuclear leukocyte chemotaxis, and complement concentrations were normal. Lymphocyte stimulation with phytohemagglutinin was low in one to two affected males and delayed skin test anergy was noted in another, raising the question of a T-lymphocyte cell abnormality. The basic genetic mechanism is unknown, but involvement of an immune response locus on the X chromosome, dysfunction of which is responsible for overactivity of the autoimmune system, is postulated.

Adult↗
PubMed1977

On the tryptic peptides from hemoglobin chains of six carnivores.

The amino acid compositions of the tryptic peptides of the following carnivore hemoglobin chains have been determined: gray fox (Urocyon cineroargenteus); raccoon (Procyon lotor); polar bear (Thalarctos maritimus); coati mundi (Nasua nasua) beta chain; coati mundi (Nasua narica) two beta chains; cat (Felis catus) alpha chain; and lion (Pantbera leo) beta chain. These provide a basis for future sequencing of these hemoglobins and construction of an evolutionary tree. The specific results are summarized in the following article (Stenzel and Brimhall, 1977).

Amino Acid Sequence↗
PubMed1977

Preliminary survey of carnivore hemoglobin compositions. Conclusions.

The amino acid differences among 12 beta chains and 10 alpha chains of carnivore hemoglobins are given. These hemoglobins conform to the substitution rate found for hemoglobins in general. A table compares the differences among known alpha-chain sequences when deduced from tryptic petide compositions and when taken from actual sequences. Among the carnivore hemoglobins studies, tryptic peptide compositions are about 14 % low in giving the number of sequence differences.

Amino Acid Sequence↗
PubMed1977

alpha-chain sequence of newt haemoglobin (Taricha granulosa).

The amino acid sequence of the alpha-chain of the major haemoglobin of a newt, T. granulosa, has been determined. The chain is 142 residues long and has an extra methionine at its N-terminus when compared with human alpha-chain. Most of the tryptic peptides were sequenced by a combination of the subtractive Edman method and by deduction from the compositions of overlapping fragments produced by various enzymic treatments. The sequence of two 'core' regions was obtained by automatic sequencing of large peptides produced by trypsin cleavage at arginine residues only after blockage of lysine residues by citraconylation; by cleavage between aspartic acid and proline residues with 70% formic acid, and by cyanogen bromide cleavage at methionine residues. The sequence of T. granulosa alpha-chain is compared with those of representative species from the other classes of vertebrates. The differences in alpha-chain between the classes of vertebrates are compared with the differences in this protein between an equal number of orders of mammals. This comparison allows us to conclude that the major functional and conformational features of alpha-chain have been conserved since the divergence of the classes of jawed vertebrates.

Amino Acid Sequence↗
PubMed1976

Non-random relationships among amino acids in protein sequences.

We have computed the observed distribution of amino acid pairs n, n+1 up to n, n+10 within 100 unrelated protein sequences containing a total of 14,034 amino acids. The expected distribution of the same amino acid pairs was calculated assuming that the amino acids within each sequence are arranged in random order. Statistical analysis of the data shows that amino acids in the n, n+1 and n, n+3 relationship deviate from random expectation at the 1% level of significance. These relationships are consistent with known secondary structures; however, there are no amino acid pairs which obviously contribute to the non-random result.

Amino Acid Sequence↗