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  • 1995-1999  (2)
  • 1925-1929
  • 1999  (2)
  • HPLC  (1)
  • Key words Knee  (1)
  • 1
    ISSN: 1432-2161
    Keywords: Key words Knee ; anatomy ; Knee ; MR ; Knee ; ligaments ; menisci ; and cartilage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Purpose To demonstrate variations in the meniscofemoral ligaments (ligaments of Wrisberg and Humphrey) at anatomical study and magnetic resonance (MR) imaging. Design Twenty-eight cadaveric knees were partially dissected for the examination of the meniscofemoral ligaments. One hundred knee MR examinations were reviewed by two experienced musculoskeletal radiologists. Proximal variations in the meniscofemoral ligaments at MR imaging were classified into three types according to the attachment site: type I, medial femoral condyle; type II, proximal half of the posterior cruciate ligament (PCL); type III, distal half of the PCL. Distal variations were classified into vertical or oblique types according to the orientation of the intermediate signal at the interface of the ligament and lateral meniscus. Results At anatomical study, six cases showed variations in the proximal insertion site of the meniscofemoral ligaments. At MR imaging 93 cases had one or more meniscofemoral ligaments, giving a total of 107 ligaments: 90 ligaments of Wrisberg and 17 ligaments of Humphrey. Forty-one ligaments of Wrisberg were type I, 28 type II, 19 type III, and with two indeterminate type, while 6 ligaments of Humphrey were type I and the remaining 11 were indeterminate. Seven cases showed no meniscofemoral ligament. Of the 107 meniscofemoral ligaments, the distal insertion orientation was of vertical type in 10 ligaments, oblique type in 70 and unidentified in 27. Conclusion An understanding of the high incidence of meniscofemoral ligament variations may help in the interpretation of knee MR studies.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-904X
    Keywords: calcitonin ; polyethylene glycol ; PEGylation ; peptide ; tryptic digestion ; stability ; HPLC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. To separate and characterize the different positional isomers of mono-PEGylated salmon calcitonins (mono-PEG-sCTs) and to evaluate the effects of the PEGylation site on the stability of different mono-PEG-sCTs in rat kidney homogenate. Methods. Mono-PEG-sCTs were prepared using succinimidyl carbonate monomethoxy polyethylene glycol (5,000 Da) and separated by gel-filtration HPLC followed by reversed-phase HPLC. To characterize PEGylated sCTs, matrix-assisted laser desorption ionization time of flight mass spectrometry (M ALDI-TOF MS) and reversed-phase HPLC of the trypsin digested samples were performed. Mono-PEG-sCTs and sCT in rat kidney homogenates were measured by column-switching reversed-phase HPLC with on-line detection of the radioiodinated samples using a flow-through radioisotope detector. Results. Three different mono-PEGylated sCTs were separated by reversed-phase gradient HPLC. From the MALDI-TOF MS analysis, the average molecular weight of mono-PEG-sCTs was confirmed as around 8650 Da. The presence of PEG moiety in the mono-PEG-sCTs was also manifested by the fact that the distance between two adjacent mass spectum lines was 44 Da which corresponds to PEG monomer unit. Tryptic digestion analysis demonstrated that these mono-PEG-sCTs are 3 positional isomers of N-terminus, Lys18- and Lys11-residue modified mono-PEGylated sCTs. The degradation half-life of these 3 positional isomers in rat kidney homogenates significantly increased in order of the N-terminus (125.5 min), Lys11- (157.3 min), and Lysl8-residue modified mono-PEGylated sCT (281.5 min) over the native sCT (4.8 min). Conclusions. Three positional isomers of mono-PEGylated sCTs were purified and characterized. Of these, the resistance to proteolytic degradation was highest for the Lysl8-residue modified mono-PEG-sCT. These studies demonstrate that the in vivo stability of PEGylated sCTs is highly dependent on the site of PEG molecule attachment.
    Type of Medium: Electronic Resource
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