scholarly journals Studies on mass spectrometry of metal chelates. II. Mass spectrometric investigation of thiooxine metal chelates.

1975 ◽  
Vol 23 (8) ◽  
pp. 1652-1656 ◽  
Author(s):  
YOSHINORI KIDANI ◽  
SHINOBU NAGA ◽  
HISASHI KOIKE
Keyword(s):  
Mass Spectrometry ◽  
Metal Chelates ◽  
Mass Spectrometric ◽  
Spectrometric Investigation ◽  
Mass Spectrometric Investigation

scholarly journals The conversion of 4-hydroxypyrazolo-[3,4-d]pyrimidine (allopurinol) into 4,6-dihydroxypyrazolo[3,4-d]pyrimidine (oxipurinol) in vivo in the absence of xanthine–oxygen oxidoreductase

1969 ◽  
Vol 112 (4) ◽  
pp. 527-532 ◽  
Author(s):  
R. A. Chalmers ◽  
R. Parker ◽  
H A Simmonds ◽  
W. Snedden ◽  
R. W. E. Watts
Keyword(s):  
Mass Spectrometry ◽  
Xanthine Oxidase ◽  
Infrared Spectra ◽  
Metabolic Pathway ◽  
Mass Spectra ◽  
Mass Spectrometric ◽  
Spectrometric Investigation ◽  
Mass Spectrometric Investigation ◽  
Congenital Deficiency

1. A patient with congenital deficiency of xanthine oxidase (EC 1.2.3.2) (xanthinuria) excreted the xanthine isomer 4,6-dihydroxypyrazolo[3,4-d]pyrimidine (oxipurinol) in his urine when the hypoxanthine isomer 4-hydroxypyrazolo[3,4-d]pyrimidine (allopurinol) was given by mouth. 2. The identity of the oxipurinol that the patient excreted was established by mass spectrometry. 3. The mass spectra and infrared spectra of allopurinol, oxipurinol, hypoxanthine and xanthine are compared. 4. A mechanism for the fragmentation of these compounds that occurs during their mass-spectrometric investigation is proposed. 5. A possible metabolic pathway for the oxidation of allopurinol to oxipurinol in the absence of xanthine oxidase is discussed.

scholarly journals A mass-spectrometric investigation of the mechanism of the semisynthetic transformation of pig insulin into an ester of insulin of human sequence

1984 ◽  
Vol 220 (1) ◽  
pp. 189-196 ◽  
Author(s):  
K Rose ◽  
J Gladstone ◽  
R E Offord
Keyword(s):  
Mass Spectrometry ◽  
New York ◽  
Oxygen Isotope ◽  
Carbonyl Group ◽  
Mass Spectrometric ◽  
Spectrometric Investigation ◽  
Mass Spectrometric Investigation ◽  
Alanine Residue ◽  
Human Sequence ◽  
Ester Product

In the trypsin-mediated semisynthetic transformation of pig insulin into an ester of insulin of human sequence, the B30 alanine residue of the pig hormone is replaced by an ester of threonine. The mechanism of this reaction was investigated by carrying out the transformation in a medium containing water enriched with 18O. Subsequent analysis by combined g.l.c.-mass spectrometry demonstrated that the oxygen isotope, is incorporated into the B29 carbonyl group of the insulin ester product. This result, together with those of appropriate controls, supports the conclusion that the transformation occurs, in the system studied, by a mechanism involving hydrolysis followed by coupling, and not by direct transpeptidation as has been previously found the case for another such system [Markussen & Schaumberg (1983) in Peptides 1982 (Bláha & Malon, eds.), pp. 387-394, W. de Gruyter, Berlin and New York].

ChemInform Abstract: Mass-Spectrometric Investigation of Ring-Chain Tautomers of 3-Amino(hydroxy)pyrazolidines.

ChemInform ◽  
1987 ◽  
Vol 18 (18) ◽  
Author(s):  
A. G. KALADARISHVILI ◽  
P. B. TERENT'EV ◽  
S. V. AFANAS'EVA ◽  
L. A. SVIRIDOVA ◽  
R. R. RAZAKOV ◽  
...  
Keyword(s):  
Mass Spectrometric ◽  
Spectrometric Investigation ◽  
Mass Spectrometric Investigation

Mass spectrometric investigation of the ionic polymerization in gaseous ethylenimine

1970 ◽  
Vol 66 ◽  
pp. 1464 ◽  
Author(s):  
A. Giardini-Guidoni ◽  
A. Mele ◽  
F. Vecchio Cattivi ◽  
F. Zocchi
Keyword(s):  
Mass Spectrometric ◽  
Spectrometric Investigation ◽  
Mass Spectrometric Investigation
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