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  • 1
    Electronic Resource
    Electronic Resource
    Differentiation of isomeric conjugated bile acids using positive-ion B/E linked scans (1991)
    s.l. : American Chemical Society
    Analytical chemistry 63 (1991), S. 247-250 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac00003a011
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  • 2
    Electronic Resource
    Electronic Resource
    Alleles at four HLA class II loci determined by oligonucleotide hybridization and their associations in five ethnic groups (1991)
    Springer
    Immunogenetics 34 (1991), S. 299-312 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The use of polymerase chain reaction (PCR) and oligonucleotide hybridization offers a new approach for the definition of HLA class II alleles. It has been possible to determine 43 alleles of DRB1, four of DRB3, two of DRB4, four of DRB5, eight of DQA1, and 14 of DQB1. These alleles are inherited together in members of families and form closely associated groups which are found repeatedly and in characteristics patterns in different populations. We have determined the HLA class II alleles and analyzed their association in 431 healthy unrelated subjects including 161 North American Caucasians, 53 Latin Americans, 61 Blacks, 88 Chinese, and 68 Israeli Jews. For-locus haplotypes (DRB1; DRB3/4/5; DQA1; DQB1) were derived from 79 B cell lines and the analysis of segregation in 34 nuclear families. The B-cell lines yielded 37 and the families showed the same, and 20 other, haplotypic combinations. In addition to these 57 haplotypes, associated alleles were assigned in the unrelated panels following certain rules. The resulting haplotypes were assigned to groups known to share associated alleles. The groups were: (1) DR1, DR2, and DRw10 (13 haplotypes); (2) DR3 and DRw6 (26 haplotypes); (3) DR5 and DRw8 (24 haplotypes); (4) DR4, DR7, and DR9 (24 haplotypes). Their distribution in populations with different ethnic backgrounds was analyzed. The expressed DRB4 allele and its null mutant were determined by PCR and oligonucleotide hybridization. The different DR7 haplotypes resulting from these determinations were analyzed in a panel of 130 North American Caucasoids. This comprehensive analysis of class II HLA haplotypes in human populations should be useful in understanding the role of these genes and in various applications including anthropolgy, disease susceptibility, and transplantation of allogeneic organs and tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00211994
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  • 3
    Electronic Resource
    Electronic Resource
    HLA-DPB1 alleles in a population from South China (1993)
    Springer
    Immunogenetics 37 (1993), S. 251-256 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Using the polymerase chain reaction (PCR) and hybridization with oligonucleotide probes, we analyzed the distribution of DPB1 alleles in 99 healthy unrelated individuals from the city of Guangzhou (Canton), South China. Twelve different DPB1 alleles were found in this panel. The most common allele was DPB1*0501 (62.6%). Other major alleles detected included DPB1*02 (DPB1*0201 and DPB1*0202), DPB1*1301, DPB1*0401, and a recently described allele, designated DPB1*2101. The hybridization pattern of DPB1*2101 showed that this allele shared sequences with DPB1*0301 and DPB1*0601 in the A and F hypervariable regions, while the C, D, and E regions were identical to those of DPB1*0202. DPB1*2101 was observed in 11% of the subjects tested. It was found to be in strong linkage dis-equilibrium with DRB1*1202. In family studies, segregation of the haplotype DRB1*1202, DRB3*0301, DQA1*0601, DQB1*0301, DPB1*2101 was observed. The second exon of DPB1*2101 was sequenced from codon 8 to codon 90 and the sequence, inferred from the pattern of hybridization, was confirmed. DPB1*0301, DPB1*0402, DPB1*0101, DPB1*1401, DPB1*1901, and another recently recognized allele, now designated DPB1*2401, were detected with low frequencies. DPB1*2401 had the same hybridization pattern as DPB1*0501 except for a probe that matches codons 85–90. In this region, DPB1*2401 encoded the amino acid sequence GPMTLQ instead of EAVTLQ as in DPB1*0501.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00187450
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  • 4
    Electronic Resource
    Electronic Resource
    Assignment of all four disulfide Bridges in echistatin (1993)
    Springer
    The protein journal 12 (1993), S. 759-764 
    Details
    ISSN: 1573-4943
    Keywords: Echistatin ; disulfide bonds ; ionspray mass spectrometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Echistatin is a 49-amino-acid protein fromEchis carinatus venom. It contains four disulfide bonds. Since the disulfide bonding is critical for biological activity, it is very important to assign the disulfide linkage in this protein. Echistatin was incubated in 250 mM oxalic acid at 100°C for 4 hr under nitrogen. Under these conditions, many overlapping disulfide-containing peptides were identified by ionspray mass spectrometry. Ionspray MS/MS data indicate that the four disulfide bonds are Cys 2–Cys 11, Cys 7–Cys 32, Cys 8–Cys 37, and Cys 20–Cys 39. To our knowledge, this is the first time all four disulfide bonds in echistatin have been assigned in one experiment without disulfide bond exchange. This approach, which combines oxalic acid hydrolysis and ionspray MS/MS, may be very useful for assigning disulfide bridges in other proteins from the disintegrin family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024934
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  • 5
    Electronic Resource
    Electronic Resource
    Primary structure of rabbit lens α-crystallins (1993)
    Springer
    The protein journal 12 (1993), S. 93-101 
    Details
    ISSN: 1573-4943
    Keywords: Rabbit lens α-crystallins ; mass spectrometry ; phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The primary structure and posttranslational modifications of rabbit lens α-crystallins were examined using electrospray ionization mass spectrometry to determine the molecular weights of the intact proteins and fast atom bombardment mass spectrometry to analyze proteolytic digests of the αA- and αB-crystallins. The previously determined primary structure of αA-crystallin was confirmed. Posttranslational modifications detected included one phosphorylation site and the presence of a truncated form minus the five C-terminal residues. The previously undetermined amino acid sequence of rabbit αB-crystallin was determined to be the same as the bovine αB-crystallin sequence except at three residues: Thr 40, Thr 132, and Pro 153. Rabbit αB-crystallin showed evidence of phosphorylation at the same three sites as bovine αB-crystallin. The molecular weights of the intact proteins indicated that any one molecule had a maximum of two phosphorylations. Also, there was a truncated form which did not include the five C-terminal residues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024920
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  • 6
    Electronic Resource
    Electronic Resource
    Identification of disulfide-containing peptides in endocrine tissue extracts by HPLC-electrochemical detection and mass spectrometry (1990)
    Springer
    The protein journal 9 (1990), S. 151-157 
    Details
    ISSN: 1573-4943
    Keywords: Electrochemical detector ; disulfide-containing peptides ; pancreas ; pituitary ; oxytocin ; somatostatin ; insulin ; mass spectrometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A new procedure to selectively identify disulfide-containing peptides in extracts of biological tissues is described. Disulfide-containing peptides are detected by their UV absorbance and electrochemical (EC) activity after chromatographic separation, and subsequently identified by fast atom bombardment mass spectrometry (FABMS). This combination of fractionation by HPLC and selective detection is attractive because it is rapid, highly specific for disulfide-containing peptides, and applicable to all disulfide-containing peptides that may be present in complex biological mixtures. Useful procedures for applying the method are demonstrated with tissue extracts from bovine pituitary and catfish pancreas. In addition to finding the expected disulfide-containing peptides, evidence for two forms of catfish insulin are presented. The merits of this and other methods used to detect peptides in similar tissue extracts are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025306
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  • 7
    Electronic Resource
    Electronic Resource
    Sequencing of Gel-Isolated Proteins Using Microblotter Capillary Liquid Chromatography-Electrospray Mass Spectrometry (1999)
    Springer
    The protein journal 18 (1999), S. 337-347 
    Details
    ISSN: 1573-4943
    Keywords: Capillary HPLC-MS ; protein sequencing ; microblotter ; gel electrophoresis ; electrospray mass spectrometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Enzymatic digests of proteins isolated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) were separated by capillary high-performance liquid chromatography (HPLC). The column eluate was split to an electrospray mass spectrometer on one side and to both a UV detector and a microblotter on the other side. Using the microblotter, the peptides eluted from the column were collected directly onto a polyvinylidene difluoride (PVDF) membrane for Edman sequencing. Thus, a peptide mass map from the mass spectrometric analysis and a prepared PVDF membrane for subsequent Edman sequencing were generated in a single experiment. The addition of molecular mass information to the blotted LC eluate is useful for determining the most important peaks to undergo Edman sequencing. Coupling the capillary HPLC with a microblotter to electrospray mass spectrometry provides an integrated system for separation, collection, and structural analysis of protein digests. It provides high levels of sensitivity, recovery, and convenience for protein characterization. Proteins loaded onto SDS–PAGE at low picomole levels can be analyzed by the new integrated system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1021095613993
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  • 8
    Electronic Resource
    Electronic Resource
    Glutathione adducts, not carbamylated lysines, are the major modification of lens α-crystallins from renal failure patients (1995)
    Springer
    The protein journal 14 (1995), S. 179-188 
    Details
    ISSN: 1573-4943
    Keywords: Lens crystallins ; renal failure ; cataract ; glutathione ; carbamylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract α-Crystallins from the water-soluble and the water-insoluble, guanidine-soluble portions of lenses from four renal failure patients and two normal donors of similar age were isolated and enzymatically digested into peptides. Molecular weights of the peptides, determined by fast atom bombardment mass spectrometry, indicated modifications specifically associated with renal failure. The only modifications observed in theα-crystallins from renal failure patients, but not in the normal old lenses, were glutathione adducts to Cys 131 and Cys 142. These adducts were present in the lenses of all four renal failure patients, but not in the two normal old lenses. The four lenses from the renal failure patients were searched for evidence of carbamylation at lysyl or cysteinyl residues: carbamylation was not detected. Because the same mass spectrometric methods had previously demonstrated sufficient sensitivity and specificity to detect as little as 5% modification in the examination ofin vitro carbamylated bovine lenses, these results indicated that carbamylation is not a major modification of the lensα-crystallins of renal failure patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01980330
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