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Y Q Tang

Publications and source records attributed to Y Q Tang.

15 recordsLinked to original sources
PubMed1995

Synthesis and characterization of indolicidin, a tryptophan-rich antimicrobial peptide from bovine neutrophils.

Indolicidin, a novel tryptophan-rich microbicidal tridecapeptide amide isolated originally from granules of bovine neutrophils, has been prepared by optimized manual and automated protocols of stepwise solid-phase synthesis with N alpha-9-fluorenylmethyloxycarbonyl (Fmoc) amino acid derivatives. Both standard polystyrene (PS) and polyethylene glycol-polystyrene (PEG-PS) graft supports were used in combination with handles that provide C-terminal peptide amides: 5-(4-Fmoc-aminomethyl-3,5-dimethoxyphenoxy)valeric acid (PAL) or 5-(9-Fmoc-aminoxanthen-2-oxy)valeric acid (XAL). Final deprotection/cleavage was carried out with reagent K, trifluoroacetic acid-phenol-water-thioanisole-1,2-ethanedithiol (82.5:5:5:5:2.5), or reagent B, trifluoroacetic acid-phenol-water-tri(isopropyl)silane (88:5:5:2), and related cocktails. Initial purities as high as 93% were obtained immediately following cleavage. In the largest-scale synthesis carried out, 0.8 g of HPLC-purified indolicidin (> 99% pure) was obtained, representing a 39% overall yield based on C-terminal Arg(Pmc) anchored to PAL-PS-resin. The main synthetic product, and some by-products, were characterized by analytical high-performance liquid chromatography (HPLC), sequencing, and fast atom bombardment mass spectrometry (FABMS). The antimicrobial potencies of natural and synthetic indolicidin, as determined by in vitro antibacterial and antifungal assays, were identical. Further, the reactivities of natural and synthetic peptides with anti-indolicidin antibody were indistinguishable.

Animals↗
PubMed1992

Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils.

A potent and structurally novel antimicrobial peptide was purified from the cytoplasmic granules of bovine neutrophils. Suspensions of Staphylococcus aureus and Escherichia coli were virtually sterilized by the peptide at a concentration of 10 micrograms/ml. The peptide was found to be comprised of 13 amino acids, 5 of which were tryptophan residues, and the carboxyl-terminal arginine was carboxamidated. The primary structure of the peptide, which we have named indolicidin, is H-Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2. The mole percent of tryptophan in indolicidin is the highest observed among known protein sequences. The multiple tryptophan residues presumably play an important role in the function of this unique antibiotic peptide.

Amino Acid Sequence↗
PubMed1992

The structural basis of the poor fibrin specificity of urokinase(I)--knowledge-based prediction of kringle structures of urokinase and its related proteins.

The Kringle-1 structure of plasminogen (PGK-1), the Kringle-2 structure of tissue plasminogen activator (PAK-2) and the Kringle structure of prourokinase (UKK) has been modeled on the basis of the three-dimensional structure of Kringle-1 of prothrombin (PTK-1) at 2.8 A resolution. The predicted three-dimensional structure of these Kringles shows that the binding site of PGK-1 is characterized by an apparent dipolar site, the polar parts of which are separated by a hydrophobic region. PAK-2 possesses the anionic center but has not a cationic binding center which might be provided by a guanidinium group from Arg-69 located adjacent to the Arg-71 position. UKK possesses neither the anionic binding center nor the cationic center which are probably the main reason for the poor fibrin specificity of urokinase.

Amino Acid Sequence↗
PubMed1990

Isolation, chemical and biological characterization of margaratensin, a neurotensin-related peptide from the skin of Rana margaratae.

A new neurotensin (NT)-related peptide, margaratensin, was obtained by Sep-Pak C18 and RP-HPLC from methanol extracts of the skin of Chinese frog Rana margaratae. The structure of the peptide has been determined to be Asp-Lys-Arg-Pro-Tyr-Ile-Leu-His-Glu, which is found to be homologous to the COOH-terminal sequence of NT, but has an extra His-Glu at the COOH-terminus. The synthetic preparation was shown to be indistinguishable from the native peptide during HPLC, amino acid analysis and bioassay. Margaratensin exhibited a hypotensive effect in the rat but the response was weaker than NT. The peptide could induce a potent and reproducible contractile activity on GPI which was different from xenopsin, another NT-related peptide from amphibian skin.

Amino Acid Sequence↗
PubMed1990

A case of heterotopic transplantation after bilateral traumatic above-knee amputations.

This paper describes a case in which a young woman's two lower limbs were crushed and amputated from the upper part of the thighs by a train. She was in serious hypovolemic shock at the time. With rapid infusion of intravenous fluids, she recovered from shock quickly, avoiding acute renal failure and ARDS. Heterotopic transplantation was performed. Two years later, the limb which had undergone heterotopic transplantation had partly restored function.

Adult↗
PubMed1990

Synthesis and biological activity of a new frog skin peptide, ranamargarin.

A new frog skin peptide, ranamargarin depicted as H-Asp-Asp-Ala-Ser-Asp-Arg-Ala-Lys-Lys-Phe-Tyr-Gly-Leu-Met-NH2' was synthesized by the conventional method. Comparisons of chemical and biological properties of both the synthetic and natural ranamargarins indicated that they were identical, so the chemical structure of ranamargarin was confirmed. Preliminary pharmacological study showed that ranamargarin was highly selective towards the SP-P subtype receptor.

Amino Acid Sequence↗
PubMed1989

Isolation and structure of ranamargarin, a new tachykinin from the skin of Chinese frog Rana margaratae.

A new tetradecapeptide, ranamargarin, has been isolated by Sep-Pak C18 and HPLC from methanol extracts of the skin of the Chinese frog Rana margaratae. The sequence of the peptide is: Asp-Asp-Ala-Ser-Asp-Arg-Ala-Lys-Lys-Phe-Tyr-Gly-Leu-Met-NH2. This structure has been confirmed by synthesis. The peptide is the largest among the amphibian tachykinins and its N-terminal amino acids are quite different from those of the other tachykinins. The formation of the sulfoxide and peak-splitting of ranamargarin during purification procedures are briefly discussed.

Amino Acid Sequence↗
PubMed1987

Crystal structure determination of mung bean trypsin inhibitor Lys fragment-bovine trypsin complex--molecular replacement, electron density map at 3.0 angstron resolution.

The orientation and position of the trypsin molecule in the complex crystal cell mung bean trypsin inhibitor Lys fragment (MBILF)-bovine trypsin (BTRY) have been successfully determined by molecular replacement method with the model of the refined bovine trypsin molecule. Starting from the BTRY coordinates which were oriented and located in the correct azimuth and position in the complex cell according to the result from rotation function and translation function, sim-weighted Fourier map with coefficients 2/Fo/-/Fc/ at 3.0 A resolution was calculated. Besides the electron density which is obviously attributed to itself, in the vicinity of the active site of BTRY the dense contour levels corresponding to the MBILF and and its boundary could be clearly seen in this map. The size of MBILF was approximately estimated at 15 x 15 x 25 A.

Crystallography↗
PubMed1985

Dermorphin-like immunoreactivity in guinea pig and rat stomach.

Dermorphin is an opioid peptide containing one D-amino acid isolated from amphibian skin. We examined the presence of dermorphin-like immunoreactivity (DMP-IR) in mammalian brain and tissues using an antiserum developed in our own laboratory which works at a dilution of 1:120,000 for Radioimmunoassay (RIA) and can detect 2.1 pg of dermorphin. We were unable to find DMP-IR in guinea pig, rat and toad brain and rat and toad spinal cord either extracted with methanol or with HCl. The guinea pig and rat stomach contained significant amounts of DMP-IR (228.9 pg/mg protein and 97.5 pg/mg protein respectively) when extracted with HCl but not with methanol. The DMP-IR we detected in the stomach is not dermorphin per se. A single peak of DMP-IR was found on Sephadex G-25 gel filtration. When re-chromatographed on reverse phase HPLC, this peak of DMP-IR gave rise to three peaks of DMP-IR.

Animals↗
PubMed1985

The study of spectra and X-ray crystal structure of a novel bionics insecticide--(CH3)2NHCH(CH2S2O3)2Na X H2O.

IR and NMR spectra of novel bionics insecticide--C5NS4O6H12Na X H2O have been studied. The molecular and crystal structures of the compound also have been determined. The compound crystallizes in the monoclinic space group C5(2)h-P21/n with a = 8.0972(9)A, b = 16.262(4)A, c = 10.370(3)A, beta = 94.26(2)degrees and z = 4. The result shows that N atom in this compound captures a proton to form HN+ group, Na+ is in statistical disorder. Therefore, the structural formula of the compound is (CH3)2HN+-CH(CH2S2O3-)2 X 1/2(Na+)2 X H2O.

Bionics↗
PubMed1984

Preliminary crystallographic studies on bacterioferritin from Azotobacter vinelandii.

Bacterioferritin-cytochrome from Azotobacter vinelandii is an unusual protein containing haem groups as well as iron core like other ferritin. This paper reports the purification of bacterioferritin by affinity chromatography and the formation of brick-red crystals from a solution containing MgCl2. The crystals are optical isotropic with maximum dimensions of 0.4 X 0.4 X 0.1 mm3. The preliminary X-ray crystallographic studies have been performed. 1.5 degrees unscreened precession photographs show that the crystals of bacterioferritin belong to the cubic system, space group I432, with cell dimension 230 A. There are probably 8 molecules in one cubic unit cell and the molecule might have 32 symmetry. A molecular diameter of 115 A is derived from the packing of the molecules and a molecular weight of 826,000 is estimated for bacterioferritin.

Azotobacter↗