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D Kauffman

Publications and source records attributed to D Kauffman.

11 recordsLinked to original sources
PubMed2000

Preparation and Certification of K-411 Glass Microspheres.

The production and characterization of NBS K-411 glass microspheres in the 2-40 µm range for certification as NIST Standard Reference Material(R) 2066 (SRM(R)) are described. Quantitative analysis and heterogeneity testing of the microspheres were done with an electron probe microanalyzer-X-ray energy dispersive spectrometry (EPMA-EDS) automated particle analysis procedure. Results for the trimmed and normalized data produced mean compositions for the elements Mg, Si, Ca, Fe, and O (calculated from stoichiometry) that are in good agreement with the certified values for the K-411 bulk glass (NBS SRM 470 Glasses for Mineral Analysis), but with uncertainties about twice as large as those for the bulk material. Differences from the bulk are attributable to microsphere geometry as well as mass and size effects.

Journal Article↗
PubMed1992

Evidence for G proteins in rat parotid plasma membranes and secretory granule membranes.

G proteins were identified in rat parotid plasma membrane-enriched fractions and in two populations of isolated secretory granule membrane fractions. Both [32P]ADP-ribosylation analysis with bacterial toxins and immunoblot analysis with crude and affinity-purified antisera specific for alpha subunits of G proteins were utilized. Pertussis toxin catalysed the ADP-ribosylation of a 41 kDa substrate in the plasma membrane fraction and both secretory granule membrane fractions. Cholera toxin catalysed the ADP-ribosylation of two substrates with molecular masses of 44 kDa and 48 kDa in the plasma membrane fraction but not in the secretory granule fractions. However, these substrates were detected in the secretory granule fractions when recombinant ADP-ribosylating factor was present in the assay medium. Immunoblot analysis of rat parotid membrane fractions using both affinity-purified and crude antisera revealed strong immunoreactivity of these membranes with anti-Gs alpha, -Gi alpha 1/alpha 2 and -Gi alpha 3 sera. In contrast Gs alpha was the major substrate found in both of the secretory granule fractions. Granule membrane fractions also reacted moderately with anti-Gi alpha 3 antiserum, and weakly with anti-Gi alpha 1/alpha 2 and -G(o) alpha sera. The results demonstrate that the parotid gland membranes express a number of G proteins. The presence of G proteins in secretory granule membranes suggests that they may play a direct role in regulating exocytosis in exocrine glands.

Adenosine Diphosphate Ribose↗
PubMed1992

Role of tumor necrosis factor in oxygen toxicity.

mRNA from lungs of mice exposed to high-dose oxygen (greater than 95%) for 3 days demonstrated increased expression of the genes for tumor necrosis factor (TNF), interleukin-1, and interleukin-6 compared with mRNA from lungs of mice exposed to room air. Daily treatment of mice exposed to high-dose oxygen with an antibody to TNF improved survival compared with mice receiving a similar dose of control immunoglobulin G. Pretreatment of mice with repetitive sublethal intraperitoneal doses of recombinant human TNF for 3 days or a single intravenous dose followed by exposure to high-dose oxygen afforded a significant survival advantage compared with high-dose oxygen-exposed mice pretreated with vehicle or interleukin-1. The repetitive intraperitoneal TNF pretreatment reduced the development of interstitial pneumonitis, pulmonary edema, and lung weight gain associated with oxygen toxicity and enhanced expression of the gene for the free radical protective enzyme manganous superoxide dismutase in lung tissue, a gene that is augmented as mice are exposed to high-dose oxygen. Furthermore a single intravenous dose of TNF 24 h after oxygen exposure was still protective. The results suggest that the toxicity of oxygen therapy can be partially ameliorated by either treatment with anti-TNF antibody or pretreatment and early treatment with TNF. These findings are consistent with the hypothesis that oxygen exposure induces TNF, which causes part of the toxicity of high-dose oxygen, and that pretreatment or early treatment with TNF induces the gene for an enzyme that recently has been shown to be very effective in protecting mice from the toxicity of oxygen.

Animals↗
PubMed1988

An in vitro analysis of wrist motion: the effect of limited intercarpal arthrodesis and the contributions of the radiocarpal and midcarpal joints.

Radiocarpal and intercarpal arthrodeses were simulated in 12 fresh cadaver wrists by means of external fixation. Range-of-motion measurements were made before and after simulated arthrodesis and used to calculate the contribution of the midcarpal and radiocarpal joints to wrist motion, as well as the residual wrist motion after limited intercarpal arthrodeses. Relative contributions to wrist motion were as follows: wrist flexion: radiocarpal (RC) joint 63%, midcarpal (MC) joint 36%; wrist extension: RC joint 53%, MC joint 46%. The wrist motion remaining after simulated arthrodeses was as follows: capitate-hamate: flexion (Flx) 98%, extension (Ext) 92%, ulnar deviation (UD) 96%, radial deviation (RD) 90%; scaphoid-lunate: Flx 97%, Ext 91%, UD 90%, RD 91%; scaphoid-trapezium-trapezoid: Flx 86%, Ext 88%, UD 67%, RD 69%; scaphoid-lunate-triquetrum: Flx 91%, Ext 82%, UD 86%, RD 70%; capitate-lunate: Flx 70%, Ext 59%, UD 89%, RD 79%; capitate-hamate-triquetrum: Flx 88%, Ext 79%, UD 88%, RD 81%; hamate-triquetrum: Flx 90%, Ext 85%, UD 89%, RD 94%; scaphoid-trapezium-trapezoid-capitate: Flx 85%, Ext 77%, UD 64%, RD 57%.

Arthrodesis↗
PubMed1986

Basic proline-rich proteins from human parotid saliva: complete covalent structures of proteins IB-1 and IB-6.

The complete amino acid sequences of two basic proline-rich proteins, IB-1 and IB-6, from human parotid saliva have been determined. Fragments for sequence analysis were obtained by enzymatic digestions. The proteins have molecular weights of 9571 (IB-1) and 11,530 (IB-6) and contain 34 and 39 mol % proline, respectively. IB-1 and IB-6 contain an identical sequence of 54 residues except for an alanine in position 52 of IB-6, where IB-1 has proline. An unusually high number of repeated sequences occurs in both molecules. IB-1 has a blocked amino-terminal residue, pyroglutamic acid, and also contains one phosphoserine residue in position 8. The relationship of these proteins to the basic proline-rich protein IB-9 [Kauffman, D., Wong, R., Bennick, A., & Keller, P. (1982) Biochemistry 21, 6558-6562] and to other salivary proline-rich proteins is discussed.

Amino Acid Sequence↗
PubMed1982

Basic proline-rich proteins from human parotid saliva: complete covalent structure of protein IB-9 and partial structure of protein IB-6, members of a polymorphic pair.

The complete amino acid sequence of a basic proline-rich protein, IB-9, from human parotid saliva was determined by automated Edman degradation of peptides obtained by enzymatic cleavage of the intact protein with clostripain. The protein was digested with papain and elastase to obtain overlapping peptides. Automated Edman degradation of the intact protein was also performed. The protein consists of 61 amino acids, of which 26 are proline residues. The partial sequence of another human parotid basic proline-rich protein, IB-6, was also obtained. With one exception the first 54 residues of the two proteins are identical. An exceptional degree of internal reiteration occurs in both molecules, including several repeated sequences of 12-14 amino acids. The proteins show a high degree of homology with the C-terminal portion of the salivary acidic proline-rich protein C.

Amino Acid Sequence↗
PubMed1979

The primary structure of calf chymosin.

The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously (Pedersen, V.B., and Foltmann, B. (1975) Eur. J. Biochem. 55, 95-103), thus we are now able to account for the total 365 amino acid residues of calf prochymosin. Comparison of the sequence of calf prochymosin with that of pig pepsinogen A (EC 3.4.23.1) shows extensive homology. In the precursor part of the sequence, 15 residues are located at identical positions, as compared to 189 identical residues in the respective enzymes. Furthermore comparison to Penicillium janthinellum acid proteinase (penicillopepsin) (EC 3.4.23.7) shows that 76 residues are common to this enzyme and to the two gastric proteinases. These homologies in sequence further suggest that the folding of the peptide chain in chymosin is very similar to that of other acid proteinases.

Amino Acid Sequence↗
PubMed1977

The complete amino acid sequence of prochymosin.

The total sequence of 365 amino acid residues in bovine prochymosin is presented. Alignment with the amino acid sequence of porcine pepsinogen shows that 204 amino acid residues are common to the two zymogens. Further comparison and alignment with the amino acid sequence of penicillopepsin shows that 66 residues are located at identical positions in all three proteases. The three enzymes belong to a large group of proteases with two aspartate residues in the active center. This group forms a family derived from one common ancestor.

Amino Acid Sequence↗