TY - JOUR
T1 - Enzymological studies of melanin concentrating hormone (MCH) and related analogues
AU - Ana, Ana Maria
AU - Visconti, Maria A.
AU - Matsunaga, Terry O.
AU - Hadley, Mac E.
AU - Hruby, Victor J.
N1 - Funding Information:
U.S. Acknowledgements--This Public Health Service work (AM kM 17420, VJH), National : was partially supported by Science Foundation (DCB86-15603 and by 5-15603, MEH), FAPESP (89/3780-6, AMLC),, and CNPq (410227/90-0, AMLC).
PY - 1992/10
Y1 - 1992/10
N2 - 1. 1. Salmon melanin concentrating hormone (MCH) is a cyclic heptadecapeptide possessing the following primary structure: Asp-Thr-Met-Arg-Cys-Met-Val-Gly-Arg-Val-Tyr-Arg-Pro-Cys-Trp-Glu-Val. 2. 2. In the fish, Synbranchus marmoratus, skin bioassay MCH5-15 is equipotent to MCH whereas MCH5-14, which comprises only the ring structure, is about 100-fold less active. 3. 3. MCH and two fragment analogues, MCH5-15 and MCH5-14, were studied to determine their relative stability in the presence of fish serum and purified proteolytic enzymes, trypsin and alpha-chymotrypsin. 4. 4. After 4 hr incubation in fish serum, MCH5-15 retained 1/100, MCH5-14 1/1000 and MCH only 6/1000 of the potency of the native hormone. 5. 5. The three peptides were also very resistant to degradation by purified proteolytic enzymes involving the following relative order of resistance: MCH5-14 > MCH5-15 > MCH. MCH5-14 potency was not altered after a 1 hr incubation in either enzyme whereas MCH retained 1/10 and 4/100 of its original potency, and MCH5-15 retained 1/10 and 8/10 of its original potency, after 1 hr in trypsin and alpha-chymotrypsin, respectively.
AB - 1. 1. Salmon melanin concentrating hormone (MCH) is a cyclic heptadecapeptide possessing the following primary structure: Asp-Thr-Met-Arg-Cys-Met-Val-Gly-Arg-Val-Tyr-Arg-Pro-Cys-Trp-Glu-Val. 2. 2. In the fish, Synbranchus marmoratus, skin bioassay MCH5-15 is equipotent to MCH whereas MCH5-14, which comprises only the ring structure, is about 100-fold less active. 3. 3. MCH and two fragment analogues, MCH5-15 and MCH5-14, were studied to determine their relative stability in the presence of fish serum and purified proteolytic enzymes, trypsin and alpha-chymotrypsin. 4. 4. After 4 hr incubation in fish serum, MCH5-15 retained 1/100, MCH5-14 1/1000 and MCH only 6/1000 of the potency of the native hormone. 5. 5. The three peptides were also very resistant to degradation by purified proteolytic enzymes involving the following relative order of resistance: MCH5-14 > MCH5-15 > MCH. MCH5-14 potency was not altered after a 1 hr incubation in either enzyme whereas MCH retained 1/10 and 4/100 of its original potency, and MCH5-15 retained 1/10 and 8/10 of its original potency, after 1 hr in trypsin and alpha-chymotrypsin, respectively.
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U2 - 10.1016/0305-0491(92)90298-6
DO - 10.1016/0305-0491(92)90298-6
M3 - Article
C2 - 1424563
AN - SCOPUS:0026707476
SN - 0305-0491
VL - 103
SP - 317
EP - 320
JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
IS - 2
ER -