Electrospray ionization mass spectrometric analysis of blood for differentiation of species

被引:35
作者
Espinoza, EO [1 ]
Lindley, NC
Gordon, KM
Ekhoff, JA
Kirms, MA
机构
[1] Natl Fish & Wildlife Forens Lab, Ashland, OR 97520 USA
[2] So Oregon Univ, Ashland, OR 97520 USA
关键词
D O I
10.1006/abio.1998.3048
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The National Fish and Wildlife Forensic Laboratory is responsible for the determination of species of birds, reptiles, and mammals from the United States, as well as international species falling under the protection of CITES treaties. We have recently found electrospray ionization mass spectrometry to be an effective means of rapidly analyzing blood samples fdr species identification. Nearly 1000 Individuals were analyzed which comprised 62 species represented by birds, mammals, and reptiles. Whole blood and dried blood samples were analyzed without purification to provide simultaneous molecular weights from the alpha- and beta-proteins present in each sample's hemoglobin. The combination of the two molecular weights for the hemoglobin proteins (i.e., alpha/beta-pairs) was used as species determining markers. In all, 133 distinctive alpha/beta-pairs were observed from the individuals analyzed. Despite the variability in the hemoglobins evaluated, 86% of these alpha/beta-pairs were found to be diagnostic for a particular species to the exclusion of all other species studied, No other single protein system studied by a single analytical technique can so effectively resolve species from a wide range of taxa as can the hemoglobin system when analyzed by electrospray ionization mass spectrometry. (C) 1999 Academic Press.
引用
收藏
页码:252 / 261
页数:10
相关论文
共 33 条
[1]   HEMOGLOBINS .83. THE PRIMARY STRUCTURE OF HEMOGLOBINS FROM THE DOMESTIC CAT (FELIS-CATUS, FELIDAE) [J].
ABBASI, A ;
BRAUNITZER, G .
BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 1985, 366 (08) :699-704
[2]   Electrospray mass spectrometry of alpha and beta chains of selected hemoglobins and their TNBA and TNB conjugates [J].
Adamczyk, M ;
Gebler, JC .
BIOCONJUGATE CHEMISTRY, 1997, 8 (03) :400-406
[3]   INTRINSIC OXYGEN-AFFINITY - THE PRIMARY STRUCTURE OF A RUMINANTIA HEMOGLOBIN - METHIONINE IN BETA-NA2 OF A PECORA, THE NORTHERN ELK (ALCES-ALCES-ALCES) [J].
ASCHAUER, H ;
WIESNER, H ;
BRAUNITZER, G .
HOPPE-SEYLERS ZEITSCHRIFT FUR PHYSIOLOGISCHE CHEMIE, 1984, 365 (11) :1323-1330
[4]   HEMOGLOBINS IN SHEEP - MULTIPLE DIFFERENCES IN AMINO ACID SEQUENCES OF 3 BETA-CHAINS AND POSSIBLE ORIGINS [J].
BOYER, SH ;
HATHAWAY, P ;
PASCASIO, F ;
ORTON, C ;
BORDLEY, J ;
NAUGHTON, MA .
SCIENCE, 1966, 153 (3743) :1539-&
[5]   HEMOGLOBINS .45. THE AMINO-ACID-SEQUENCE OF PHEASANT (PHASIANUS-COLCHICUS-COLCHICUS) HEMOGLOBINS [J].
BRAUNITZER, G ;
GODOVAC, J .
HOPPE-SEYLERS ZEITSCHRIFT FUR PHYSIOLOGISCHE CHEMIE, 1982, 363 (03) :229-238
[6]   AMINO-ACID SEQUENCE OF DOG (CANIS-FAMILIARIS) HEMOGLOBIN [J].
BRIMHALL, B ;
DUERST, M ;
JONES, RT .
JOURNAL OF MOLECULAR EVOLUTION, 1977, 9 (03) :231-235
[7]   HETEROGENEITY OF THE HEMOGLOBIN OF THE OHRID TROUT (SALMO L TYPICUS) [J].
CEPREGANOVA, B ;
WILSON, JB ;
WEBBER, BB ;
KJOVKARESKA, B ;
EFREMOV, GD ;
HUISMAN, THJ .
BIOCHEMICAL GENETICS, 1992, 30 (7-8) :385-399
[8]   GENETIC ORGANIZATION OF THE POLYMORPHIC EQUINE ALPHA-GLOBIN LOCUS AND SEQUENCE OF THE BII ALPHA-1 GENE [J].
CLEGG, JB ;
GOODBOURN, SEY ;
BRAEND, M .
NUCLEIC ACIDS RESEARCH, 1984, 12 (20) :7847-7858
[9]  
DRATCH P A, 1986, Proceedings of the New Zealand Society of Animal Production, V46, P179
[10]  
DRESLER SL, 1974, ANN NY ACAD SCI, V241, P411, DOI 10.1111/j.1749-6632.1974.tb21896.x