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blacktarotannis;4675005; said:
Thoses loaches you have are nice I was thinking of getting one.

yup, they are nice very nice, but here, they're not always available. I spent months searching for just one. At last I found them in one shop then I bought them all. There is another fish which I tempted to get atm, which is the toungefish/freshwater flounder, which is also extremely hard to get here.
 
http://www.loaches.com/articles/hillstream-loaches-the-specialists-at-life-in-the-fast-lane

Please read that... hillstream loaches often appear to do OK in community tanks without any sort of special requirements, but usually die within the space of a year. I think the goal of a fish keeper should be to provide the optimum habitat to a fish anyway. These fish are all wild caught to my knowledge and come from fast flowing streams in the hills of China.
Do I need to explain why your tank is overstocked and undersized? It's tiny. Setting up my hillstream loach biotope, for just a half dozen loaches, I didn't consider anything less than a 20 gallon long. Fish need room to move too, aside from water quality issues. I'm not trying to be a jerk at all, just sharing my knowledge base and experience from keeping these fish as a hobbyist and caring for/selling them when working in the industry.
A 7 gallon tank in my opinion is only suitable for a betta.
 
Here we go:

Many of these fish have been exported from their home lands, to all over the World and countless numbers have likely perished when other fish in the same tanks may have been a picture of health. Why should this be?Logically, it is likely to be the difference in relative water movement and therefore oxygen content between the "conventional" aquarium and their home streams. Are they getting insufficient oxygen? Surely, we could just increase aeration a bit and they'd "make do"? But how come the other fish are so happy?
The answer may lie in the fact that the oxygen is carried in the blood by the respiratory pigment Hemoglobin. Oxygen can dissolve directly into the blood, but (in Humans for example) the oxygen carrying capacity of blood containing red cells full of hemoglobin is 70 times that of blood. The special feature about the binding of the oxygen to hemoglobin is, unlike in the oxidation of say, Iron (II) to Iron (III) (rusting), and over a narrow range of conditions, maintained by physiological regulation, the reaction is reversible. The pigment can easily pick up oxygen at the lungs or gills and give it up equally readily at the tissues where it is required for respiration. There is an iron ion (Fe2+) at the center of the central haem part (a type of metalloporphyrin) of the hemoglobin molecule, which is the oxygen binding site. The precisely controlled spatial inter relationship of the molecules in the surrounding globin (a variety of protein) and the resultant molecular forces act to prevent irreversible bindings. The special nature of the arrangement is evidenced by the fact that the haem group isolated from the globin will only bind with the oxygen irreversibly.
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In the gills of fish, thousands of secondary lamellae on the gill filaments are in contact with oxygen bearing water. Hemoglobin, carried within the millions of minute blood capillaries within the gill lamellae, loads up with oxygen when the oxygen content of the water surrounding the gills is relatively high and unloads its oxygen at the tissues throughout the body, where the oxygen content is lower. This loading and unloading is automatic, in response to the rising and falling relative pressure exerted by the dissolved oxygen (although it is a much more complicated process than this makes it sound!).
With rare exceptions, hemoglobin occurs in all vertebrates and many invertebrate groups. As far as is known, the haem parts are all identical, whereas the globin portions of the molecule vary. Herein lies the beginnings of the answer why these fishes struggle in captivity. Small differences in the structure of the globin portion have a dramatic effect on the physiological properties of haemoglobin. The ease with which a particular variety of hemoglobin takes up oxygen is termed 'the affinity of the haemoglobin for oxygen'. Haemoglobin is also sensitive to the level of dissolved Carbon Dioxide (CO2), and to the temperature. Relatively high CO2 levels reduce the haemoglobin's affinity for oxygen. This is but one way Evolution has exploited the properties of biochemical substances. CO2 is a waste product of of cell respiration, so CO2 levels tend to be higher in those tissues that are doing 'work', and where, therefore Oxygen is needed. The high CO2 level actually 'helps' the hemoglobin unload O2.
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Rising temperatures reduce the affinity of haemoglobin for O2. Fish are the same temperature as their water, so the decrease in affinity can be sufficient to prevent adequate loading of the pigment at the gills, especially as the fish has a low affinity pigment. This is compounded by the fish's increased demand for O2 at the higher temperatures, and by the reduced solubility of O2 as the temperature rises. Equally, falling temperature increases the haemoglobin affinity, but decreases the ease of unloading at the tissues. In other words, you can't juggle a particular species haemoglobin affinity, by altering the temperature of it's environment.
Some hemaglobins have a greater affinity for O2, and bind easier, the benefits of which are obvious. But the downside of high affinity is that it 'costs' the organism more in terms of engineering the physical circumstances conducive to unloading the O2 at the tissues. If the O2 binds easily it is harder to "unbind". With high haemoglobin affinity, a fish can inhabit low O2 level environments. Carp for example, have high affinity haemoglobin,so can inhabit still waters.
Some fishes, by contrast have adapted to waters where the O2 levels are far higher, such as fast flowing streams and the upper levels of the open sea. Here there is no need for a high affinity pigment, and such fish have evolved a low affinity pigment, that has little difficulty in binding with O2 because of it's abundance. The benefits of a low affinity pigment are in the ease with which it unloads it's O2 at the tissues, saving the of biochemically "engineering" the unloading process which other fish have to pay.
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Therefore in O2 rich waters the low affinity haemoglobin can be more efficient in getting the O2 to the tissues than a high affinity one (this concept sounds paradoxical, but is quite logical). BUT..a low affinity haemoglobin will NOT work properly in a low or only average dissolved O2 level environment.
These fish are therefore just not found in low oxygen content waters, and the average home fish tank falls somewhere into this category.
It is therefore logical to suppose that these fish have the physiological adaptation of low affinity haemoglobin and are therefore not able to survive in a tank unless it has adequate levels of dissolved O2.
 
well as usual people would rather make fun of tank size than help. i can only be certain of brown with black stripes is commonly known as tiger snail survives freshwater breed like machine in brackish and all fish in any size tank are cool
 
brutonsbrew;4677407; said:
well as usual people would rather make fun of tank size than help. i can only be certain of brown with black stripes is commonly known as tiger snail survives freshwater breed like machine in brackish and all fish in any size tank are cool

No one is making fun of anyone... I love nano tanks. But the OP stocking choices aren't appropriate for the health of the fish he has, please explain how not pointing that out would be beneficial to anyone??

You're saying we are "making fun" of tank size, but I openly keep small tanks, look at my signature... I brag about my 20 gallon ALL DAY LONG BUDDY!
 
Appropriate stock off the top of my head for a 7 gallon:

-Betta (arguable)
-Shrimp (awesome option)
-Snails
-Maybe some amphibians, but I openly admit my knowledge base lies outside this area
 
well maybe not you inpaticular but find many overly critical responses from people on a forum that is for entertainment. i also have seen your response here and other posts and i assure i did not intend for you
 
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