Appeal No. 1997-0798
Application 08/128,020
infarction. Specification, page 3. Thus, use of troponin I as a marker for the occurrence
of an infarct is problematic.
As explained at page 4 line 21- page 5 line 7 of the specification:
Surprisingly, it turned out that a significantly higher sensitivity can be
obtained by a troponin T immunoassay in the determination of myocardial
necroses (such as e.g. by cardiac infarction, ischaemia or angina pectoris)
than by the determination of other parameters such as CK, CK-MB, GOT,
LDH or troponin I. As established by the inventors the reason for this is
that in contrast to other proteins of the contractile apparatus no serum
concentration can be measured for troponin T up to the detection limit of
the test (0.25 ng/ml) in normal patients (who have not suffered myocardial
necroses).
This is particularly surprising since, because of the functional relationship
between the troponins, a similar serum concentration to that for troponin I
would be expected for troponin T. Furthermore, the serum concentration
curve of troponin T differs significantly, for example in a transmural
infarction, from the curve for troponin I. In contrast to troponin I the curve
of the time course is in three phases instead of two phases and troponin T
is found to be increased on average for up to 300 hours after the onset of
pain. The time interval for absolute diagnostic sensitivity lasts from the 6th
to the 195th hour. The time interval for the absolute diagnostic sensitivity
is thus nearly four times as long as that known for troponin I.
Appellants’ invention involves the use of an antibody to troponin T as a means to
diagnose and monitor myocardial necroses in a patient. Troponin exists in human
skeletal muscle as well as human cardiac muscle. Thus, in order to monitor myocardial
necroses it is important that an a ntibody be able to differentiate between the two
proteins. As the claims now read, all claims require the use of at least one antibody to
human cardiac muscle troponin T having cross-reactivity to human skeletal muscle
troponin T which is less than 5% as determined by ELISA and cross-reactivity to
troponin I and other myofibrillar proteins of less than 2% as determined by ELISA.
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