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  • 1
    Electronic Resource
    Electronic Resource
    Molecular Basis of Type IA (Tyrosinase Negative) Oculocutaneous Albinism (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Periodontology 2000 3 (1990), S. 0 
    Details
    ISSN: 1600-0757
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0749.1990.tb00380.x
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  • 2
    Electronic Resource
    Electronic Resource
    Analysis of Tyrosinase Mutations Associated With Tyrosinase-Related Oculocutaneous Albinism (OCAI) (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Periodontology 2000 7 (1994), S. 0 
    Details
    ISSN: 1600-0757
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Mutations of the tyrosinase gene associated with a partial or complete loss of enzymatic activity are responsible for tyrosinase related oculocutaneous albinism (OCA1). A large number of mutations have been identified and their analysis has provided in-sight into the biology of tyrosinase and the pathogenesis of these different mutations. Missense mutations produce their effect on the activity of an enzyme by altering an amino acid at a specific site. The location of these mutations in the peptide can be used to indicate potential domains important for enzymatic activity. Missense mutations of the tyrosinase polypeptide cluster in four regions, suggesting that these are important functional domains. Two of the potential domains involve the copper binding sites while the others are likely involved in substrate binding. More critical analysis of the copper binding domain of tyrosinase can be gained by analyzing the structure of hemocyanin, a copper-binding protein with a high degree of homology to tyrosinase in the copper binding region. This analysis indicates a single catalytic site in tyrosinase for all enzymatic activities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0749.1994.tb00629.x
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and Characterization of Dopachrome Tautomerase (DT) (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Periodontology 2000 3 (1990), S. 0 
    Details
    ISSN: 1600-0757
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0749.1990.tb00345.x
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of Mutations in the Copper B Binding Region Associated With Type I (Tyrosinase-Related) Oculocutaneous Albinism (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Periodontology 2000 5 (1992), S. 0 
    Details
    ISSN: 1600-0757
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Mutations of the tyrosinase gene are responsible for type I (tyrosinase-related) oculocutaneous albinism (OCA), an autosomal recessive genetic syndrome with a broad phenotypic spectrum. Mutant tyrosinase alleles can be associated with no melanin synthesis (I-A, tyrosinase-negative OCA), small to moderate amounts of melanin (I-B, yellow OCA) or unusual pigment patterns (I-TS, temperature-sensitive OCA). A total of 26 mutations of this gene have been described in type I OCA. Analysis of all known missense mutations (n = 17) shows that most cluster in three areas of the coding region. Two clusters involve the copper A or copper B binding sites and may disrupt the metal ion-protein interaction necessary for enzyme function and the third cluster is located in exon I. Computer modeling of the secondary structure of the copper binding regions based on homology with the known crystal structure of hemocyanin show that they both consist of two a helicies containing three histidine ligands that complex to a single copper atom. Mutations in the copper B binding region lie in the region between the two a helices that consists of a loop structure. These mutations may affect tyrosinase activity by either altering the position of the a helical domains and thus preventing proper copper binding to the histidine ligands, or affecting a catalytic or substrate binding site located between the two a helical domains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0749.1992.tb00549.x
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  • 5
    Electronic Resource
    Electronic Resource
    Molecular analysis of type I-A (tyrosinase negative) oculocutaneous albinism (1992)
    Springer
    Human genetics 〈Berlin〉 90 (1992), S. 258-262 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Type I oculocutaneous albinism (OCA) is caused by the reduction in or absence of activity of tyrosinase in melanocytes in skin, hair, and the eyes, the result of mutations of the tyrosinase gene. To date, a total of 22 unique mutations in the coding region of tyrosinase have been described in the literature. In this report we present 5 additional mutations of the tyrosinase gene associated with type I-A OCA in four individuals, including 2 missense, 1 frameshift and 2 nonsense mutations, and review the relevant literature on all published mutations. Analysis of the distribution of all identified missense mutations (n = 17) shows that most cluster in three areas of the gene and involve amino acids conserved between humans and the mouse. Two clusters involve the copper A and copper B binding sites and may disrupt the metal ion-protein interaction necessary for enzyme function. The third cluster in exon I could represent a functional domain important in enzyme function such as the tyrosine or the dihydroxyphenylalanine (DOPA) binding site of the enzyme. Small deletions or insertions resulting in frameshift mutations and nonsense mutations are distributed throughout the coding region and do not appear to cluster.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00220074
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  • 6
    Electronic Resource
    Electronic Resource
    Detection of a Tsp509I polymorphism in the 3′ UTR of the human tyrosinase related protein-1 (TYRP) gene (1995)
    Springer
    Human genetics 〈Berlin〉 95 (1995), S. 247-247 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We have identified a Tsp509I polymorphism in the 3′ UTR of the human tyrosinase related protein-1 gene (TYRP). TYRP is one of several genes involved in melanin pigment production.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00209417
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  • 7
    Electronic Resource
    Electronic Resource
    Analysis of tyrosinase gene mutations using direct automated infrared fluorescence DNA sequencing of amplified exons (1994)
    Weinheim : Wiley-Blackwell
    Electrophoresis 15 (1994), S. 159-164 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The ability to correctly diagnose the molecular cause of genetic diseases is becoming increasingly important in medicine. This requires an efficient method for the analysis of the DNA sequence of specific genes and the detection of mutations in affected individuals. We report a method to determine the mutations responsible for tyrosinase related albinism (OCA1) using a combination of polymerase chain reaction-single stranded conformational polymorphism (PCR-SSCP) analysis and direct DNA cycle sequencing using fluorescently labeled oligonucleotides and an automated DNA sequencer based on infrared fluorescence technology. This method allows DNA from several individuals to be sequenced quickly and simultaneously so that the specific location of each mutation and the carrier status of family members can be determined.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150150127
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  • 8
    Electronic Resource
    Electronic Resource
    Multiplexed short tandem repeat polymorphisms of the Weber 8A set of markers using tailed primers and infrared fluorescence detection (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 3079-3083 
    Details
    ISSN: 0173-0835
    Keywords: Multiplex polymerase chain reaction ; Tailed primers ; Gene mapping ; Short tandem repeat polymorphisms ; ODS ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Short tandem repeat polymorphism (STRP) markers have become important reagents for mapping genetic diseases. These markers are available as screening sets, which are located in all chromosomes at discrete intervals, allowing the entire genome to be analyzed. Mapping studies that include many individuals in the analysis necessitate the production of large numbers of genotypes. In an effort to increase the efficiency and lower the cost of using these STRP screening sets, we have divided the amplification primers of the Weber 8A screening set into groups that can be amplified in single polymerase chain reaction (PCR) amplification reactions, resulting in a reduction of both time and cost. Fluorescently-labeled amplification products were produced using a three primer reaction. The forward STRP amplification primer for each marker contained a 19 bp sequence at the 5′ end. A fluorescently-labeled primer, with a sequence identical to the 19 bp tail, was added to the amplification reaction as the sole source of fluorescent label. The STRP banding pattern is detected using an automated fluorescent DNA sequencer. Use of this multiplexed genomic screening set should greatly enhance the mapping of human disease loci.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191806
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